2. CD20
CD20 is a highly expressed surface antigen that is located mainly on pre
B and mature B lymphocytes.
● Over 95% of B-cell lymphocytes express CD20 as they develop
from their pre-B cell stage into plasma cells.
● Unlike other B-cell antigens, CD20 is not shed or internalized upon
antibody binding.
o This may allow therapeutic antibodies to recruit immune
effector cells and mediate sustained immunologic activity.
● CD20 is believed to play a role in the regulation of calcium
transport and B-cell activation and proliferation.
● CD20 is not found on early B-cell progenitors or later mature
plasma cells and is not found free in plasma.
http://www.biooncology.com/therapeutic-targets/cd20
http://www.newcomersupply.com/
3. CD31
http://www.abcam.com/cd31-antibody-ab28364.html
The endothelium of vessels of any tissues are positive.
my IHC.CD31 kidney 40x
A monoclonal antibody against the endothelial cell adhesion molecule CD31.For detection of
vascular lesions including benign and malignant vascular neoplasms.
Used with Collagen IV sometimes,they together provide a powerful tool for
1) the diagnosis of endothelial neoplasms and
2) the definition of endothelial, mural and pericytic or perivascular tissue
compartments in vascular lesions of complex architecture.
Hence, we use CD31 and type IV collagen in cases of presumed vascular neoplasms,
adding other markers to the panel in accordance with the differential diagnosis,
as well as in the recognition of compromised endothelia, such as in vascular invasion
by various malignant neoplasms. http://www.ncbi.nlm.nih.gov/pubmed/7479359
4. CD56
Function This protein is a cell adhesion molecule involved in
neuron-neuron adhesion, neurite fasciculation, outgrowth of
neurites, etc.
Sequence similarities Contains 2 fibronectin type-III domains.
Contains 5 Ig-like C2-type (immunoglobulin-like) domains.
Cellular localization Secreted and Cell membrane.
NCAM1 Antibodies
NCAM, as a member of the immunoglobulin superfamily of
adhesion molecules is characterized by several
immunoglobulin (Ig)-like domains. The extracellular part of
NCAM consists of five of these Ig domains and two fibronectin
type III homology regions. NCAM is encoded by a single copy
gene composed of 26 exons. However, at least 20-30 distinct
isoforms can be generated by alternative splicing and by
posttranslational modifications, such as sialylation. During
sialylation, polysialic acid (PSA) carbohydrates are attached to
the extracellular part of NCAM. Through its extracellular
region, NCAM mediates homophilic interactions. In addition,
NCAM can also undergo heterophilic interactions by binding
extracellular matrix components, such as laminin, or other cell
adhesion molecules, such as integrins.
Tissue control: pancreas (pos.),lung (neg.)
Synonyms CD-56, CD16A, CD16B, CD3
epsilon, CD3-epsilon, CD3e antigen, CD8a,
CD8alpha, CD8b, CD8beta, epsilon
polypeptide TiT3 complex, epsilon subunit of
T3, Fc gamma Receptor 3, Fc gamma
Receptor III, FCGR3, FCGR3A, FCGR3B,
FCGRIII, FCR-10,FCRIII,FCRIIIA,FLJ18683,
Leu-2, MAL, MSK39, NCAM, NCAM1, neural
cell adhesion molecule 1,p32,RP11-5K23.1,
T-cell antigen receptor complex, T-cell
surface antigen T3/Leu-4 epsilon chain, T-cell
surface glycoprotein CD3 epsilon chain, T3E,
5. http://www.abcam.com/cd46-antibody-epr4014-ab108307.html
ab108307, at 1/500 dilution, staining CD46
in paraffin-embedded Human tonsil tissue
CD46
ab108307 showing positive staining in
Thyroid gland carcinoma tissue.
Positive control
Molt-4, Jurkat, HeLa, and K562 cell lysates;
Human kidney and Tonsil tissue
ab108307 showing positive staining
in breast carcinoma tissue.
ab108307 showing positive
staining iin normal breast tissue.
6. Immunogen
Synthetic peptide conjugated to KLH derived from within residues
1250 to the C-terminus of Human CD45.
(Peptide available as ab17550.)
Positive control
This antibody gave a positive signal in Jurkat whole cell
lysate and Hodgkins lymphoma tissue sections.
http://www.abcam.com/cd45-antibody-ab10559.html
Leucocyte Common Antigen (LCA)
Tissue: (+) Tonsil / (-) Adipose
Function Protein tyrosine-protein phosphatase required for T-cell
activation through the antigen receptor. Acts as a positive
regulator of T-cell coactivation upon binding to DPP4. The first
PTPase domain has enzymatic activity, while the second one
seems to affect the substrate specificity of the first one. Upon
T-cell activation, recruits and dephosphorylates SKAP1 and
FYN.
Involvement in disease Defects in PTPRC are a cause of severe
combined immunodeficiency autosomal recessive T-cell-
negative/B-cell-positive/NK-cell-positive (T(-)B(+)NK(+) SCID)
[MIM:608971].
A form of severe combined immunodeficiency (SCID), a genetically
and clinically heterogeneous group of rare congenital
disorders characterized by impairment of both humoral and
cell-mediated immunity, leukopenia, and low or absent
antibody levels. Patients present in infancy recurrent,
persistent infections by opportunistic organisms. The common
characteristic of all types of SCID is absence of T-cell-
mediated cellular immunity due to a defect in T-cell
development.
Genetic variations in PTPRC are involved in multiple sclerosis
susceptibility (MS) [MIM:126200].
MS is a neurodegenerative disorder characterized by the gradual
accumulation of focal plaques of demyelination particularly in
the periventricular areas of the brain. Peripheral nerves are not
affected. Onset usually in third or fourth decade with
intermittent progression over an extended period. The cause is
still uncertain.
CD45
7. This antibody recognizes the HMW (High Molecular Weight) keratin
polypeptides of 68, 58, 56.5 and 50 kDa in extract of stratum corneum.
The antibody reacts with squamous, ductal and other complex epithelia.
It stains adenocarcinomas, breast, pancreas, bile duct, salivary gland
and transitional cell carcinomas.
HMW cytokeratin
Cytokeratins are intermediate filament keratins found in the intracytoplasmic
cytoskeleton of epithelial tissue. There are two types of Cytokeratins: the low
weight, acidic type I cytokeratins and the high weight, basic or neutral type II.
Cytokeratins are usually found in pairs comprising a type I Cytokeratin and a type
II cytokeratin.
The high molecular weight cytokeratins, which are the basic or neutral
cytokeratins, comprise subtypes CK1 (67), CK2 (65.5), CK3 (64), CK4 (59), CK5
(58), CK6 (56), CK7 (54), CK8 (52.5) and CK9.
The low molecular weight cytokeratins, which are the acidic cytokeratins,
comprise subtypes CK10 (56.5), CK12 (56), CK13 (53), CK14 (50), CK16( 48),
CK17 (46), CK18 (45), CK19(48) and CK20(46).
Cellular localization Cytoplasmic
http://www.abcam.com/hmw-cytokeratin-antibody-34be12-ab776.html
staining human skin tissue sections
by IHC-P.
human colon carcinoma stained with HMW Cytokeratin,
using ABC and AEC chromagen.
8. CAM 5.2
CloneCAM 5.2
Isotype IgG2a
Immunogen Anti-Cytokeratin, clone CAM 5.2, is derived
from hybridization of mouse P3/NS-1/1-Ag4-1myeloma
cells with spleen cells from BALB/c mice immunized with
the human colorectal carcinoma cell line HT29.
Summary Anti-Cytokeratin (CAM 5.2) reagent has a primary
reactivity with human keratin proteins that correspond to
Moll’s peptides #7 and #8, Mr 48 and 52 kilodaltons (kd),
respectively. Cytokeratin 7 and 8 are present on secretory
epithelia of normal human tissue but not onstratified
squamous epithelium. Anti-Cytokeratin (CAM 5.2) stains
most epithelial-derived tissue, including liver, renal tubular
epithelium, and hepatocellular and renal cell carcinomas.
Anti-Cytokeratin (CAM 5.2) might not react with some
squamous cell carcinomas.
Cellular Localization Cytoplasmic
Positive Control Tissue Lung, colon, prostate and breast
tissue
http://dbiosys.com/products/primary-antibodies/item/5041-cam-52-5041/5041-cam-52-5041
9. p63
Data supports a role for p63 in squamous and transitional cell carcinomas,
as well as certain lymphomas and thymomas.
The p63 gene, located on chromosome 3q27-28, is a member of the p53 gene
family. The product encoded by the p63 gene has been reported to be essential
for normal development.
p63 expression is restricted to the nucleus, with a nucleoplasmic pattern. We
also observed that the expression was restricted to epithelial cells of stratified
epithelia, such as skin, esophagus, exocervix, tonsil, and bladder, and to certain
subpopulations of basal cells in glandular structures of prostate and breast, as
well as in bronchi.
p63 is expressed predominantly in basal cell and squamous cell carcinomas, as
well as transitional cell carcinomas, but not in adenocarcinomas, including those
of breast and prostate. Interestingly, thymomas expressed high levels of p63.
Moreover, a subset of non-Hodgkin’s lymphoma was also found to express p63.
Using isoform-specific reverse transcription-PCR, we found that thymomas
express all isoforms of p63, whereas the non-Hodgkin’s lymphoma tended to
express the transactivation-competent isoforms. We did not detect p63
expression in a variety of endocrine tumors, germ cell neoplasms, or
melanomas. Additionally, soft tissue sarcomas were also found to have
undetectable p63 levels.
http://clincancerres.aacrjournals.org/content/8/2/494.full
10. p63
Representative photomicrographs of
immunophenotypes of p63 in normal thymus and
thymomas, obtained using the anti-p63 4A4
monoclonal antibody.
Strong p63 nuclear staining is observed in a
population of cells identified as the epithelial
elements of the thymus (A).
We also observed p63 immunostaining in the
neoplastic component of various thymomas,
including invasive (B and D), spindle cell (E), and
thymic carcinoma (F).
Consecutive normal thymus (not shown) and
thymoma (B andC) sections were stained with p63
(B) and the anticytokeratin AE1/AE3 monoclonal
antibody cocktail (C), revealing that the p63-
expressing cells were also costained for cytokeratins
and thus are considered of epithelial nature.
Original magnifications: ×100 for B and C;
×200 for D and E;
×400 for A and F.
11. HER2
A protein involved in normal cell growth. It is found on some types of cancer cells, including
breast and ovarian. Cancer cells removed from the body may be tested for the presence of
HER2/neu to help decide the best type of treatment. HER2/neu is a type of receptor
tyrosine kinase. Also called c-erbB-2, human EGF receptor 2, and human epidermal growth
factor receptor 2.
The HER2 gene makes HER2 proteins. HER2 proteins are
receptors on breast cells. Normally, HER2 receptors help control
how a healthy breast cell grows, divides, and repairs itself. But in
about 25% of breast cancers, the HER2 gene doesn't work
correctly and makes too many copies of itself (known as HER2
gene amplification). All these extra HER2 genes tell breast cells
to make too many HER2 receptors (HER2 protein
overexpression)
http://www.gene.com/medical-professionals/medicines/herceptin
12. It can control the growth of
cancer cells that produce too
much of a protein called HER2
(human epidermal growth
factor receptor
Some breast cancers and
stomach cancers have large
amounts of HER2 and they are
called HER2 positive cancers.
HER2 makes the cancer cells
grow and divide.
When Herceptin attaches
to HER2 it can make the cells
stop growing and die.
Trastuzamab
a monoclonal antibody
brand name : Herceptin
13. HER2 for Gastric Cancer Detection
HER2
is more than a breast cancer receptor marker; it is also a
Stomach cancer biomarker
Of those diagnosed with the disease, about 22% of people with metastatic
stomach cancer have HER2-positive (human epidermal growth factor receptor-
positive) tumors, which are more aggressive and have a poorer prognosis,
however they might be helped by Trastuzamab.
14. anti HER2 receptor Trastuzumab for
breast, stomach
Based on data from a large multicenter phase III trial (ToGA study) trastuzumab has very recently
been approved by the EMEA for metastatic gastric cancer and adenocarcinoma of the gastro-
esophageal junction. Only patients with tumors which over express Her2 as defined by IHC2+ and a
confirmatory FISH+ result, or IHC 3+, determined by an accurate and validated assay are eligible for
trastuzumab therapy. However, testing of Her2 status by immunohistochemistry (IHC) differs from
breast cancer in core aspects: 1. IHC2+/3+ is scored even though membranous staining is incomplete
if membrane staining is clearly detectable even at low magnification (2.5x/5x, 3+) or medium
magnification (10x/20x, 2+). 2. Additionally, membrane staining at the appropriate intensity found in at
least 10% of tumor cells is restricted to resection specimens. Evaluation of Her2 in situ hybridization
(ISH) is similar to breast cancer with ratio values of > or =2.0 indicating Her2 gene amplification.
Taking these modifications into account and defining the HER2 positive subgroup as IHC 3+ and
IHC2+/FISH+, approximately 16% of gastric cancers are considered Her2 positive, affecting mainly
tumor regions with intestinal (gland forming) type carcinoma. In contrast to breast cancer, up to one-
third of gastric cancers show a heterogeneous Her2 status both at IHC and ISH levels which favors
bright field ISH over FISH.
15. HER2-CONNECT™: Changing HER2 IHC analysis in important ways
http://www.visiopharm.com/news-and-events--press-releases-page.shtml?page=07-20101117-533595168
Traditional requirements to meticulous
outlining of tumor regions
Visiopharm’s patented HER2-
CONNECT™ algorithm eliminates the
need for manual outlining, leading to
time savings
Researchers can work with HER2-CONNECT™ in two different ways: 1)
Connectivity and score are immediately computed based on operator
defined regions of interest, and 2) Batch processing: Full sections
and/or Tissue Micro Arrays can be subjected to analysis in batch
processing mode. Computational efficiency makes both approaches
possible and feasible on standard desktop computers.
16. VIMENTINVimentin, a major constituent of the intermediate filament (IF) family of proteins, is
ubiquitously expressed in normal mesenchymal cells and is known to maintain cellular
integrity and provide resistance against stress. Increased vimentin expression has been
reported in various epithelial cancers including prostate cancer, gastrointestinal tumors,
CNS tumors, breast cancer, malignant melanoma, lung cancer and other types of cancers.
Vimentin's over-expression in cancer correlates well with increased tumor growth, invasion
and poor prognosis; however, the role of vimentin in cancer progression remains obscure.
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3162105/
Rat cerebral cortex cultures stained
with chicken antibody to vimentin
ab24525 (green) and rabbit
antibody to GFAP (red). Note
flattened fibroblastic cells are
mostly green (i.e. vimentin positive,
GFAP negative), while clearly
astrocytic cells, express both
vimentin and GFAP and therefore
appear golden or orange. Certain
other cells express predominantly
GFAP and therefore appear red.
Tissue: (+) Melanoma /(-) Adipose
vimentin staining of a tonsilar lymphoma.
Note that the epithelium (at the left)
is negative.
17. Melan- A
Melan-A is a melanocyte differentiation antigen, recognized by autologous cytotoxic T
lymphocytes. Melan-A is also called MART-1 (melanoma antigen recognized by T cells). The
Melan-A/MART-1 gene encodes this protein, 20-22 kDa, associated with endoplasmic
reticulum and melanosomes. The function of the protein is unknown. Melan-A is expressed in
all normal melanocytes and melanocyte cell lines.
Using the monoclonal antibody A-103, staining is also seen in steroid hormone producing
cells: adrenal cortex granulosa and theca cells of the ovary and Leydig cells of the testis. This
is due to cross reaction (as the Melan-A gene is not detected in these cells).
18. Fig. 1B. Melan-A staining of normal adrenal cortex using
mAb A103. Strong staining of the steroid producing cells.
With other melan-A Abs, steroid producing cells are
negative.
Fig. 1A. Melan-A staining of normal skin showing
strong staining of melanocytes.
Fig. 2A. Melan-A staining of skin with malignant melanoma
showing strong staining of normal and neoplastic melanocytes.
Novored is here used as chromogene to avoid the merging of
melanin and the DAB chromogene.
Fig. 2B. Melan-A staining of renal PEComa
(perivascular epitheloid cell tumour)
Fig. 2C. Melan-A (mAb A103) staining o
f adrenal cortical carcinoma.
Fig. 2D. Melan-A (mAb A103) staining
of granulosa cell tumour
http://www.nordiqc.org/Epitopes/melan-a/melan-a-figs.htm
Melan-A
19. CK5 Western Blot (WB)
1:500 - 1:2000
Immunofluorescence (IF)
1:200 - 1:1000
Immunocytochemistry
(ICC)
1:200 - 1:1000
Immunohistochemistry
(IHC)
1:200 - 1:1000
Flow Cytometry (FACS)
1:200 - 1:400
* Suggested working
dilution
http://www.pierce-antibodies.com/CK5-antibody-clone-2C2-Monoclonal--MA517057.html#
The protein encoded by this gene is a member of the keratin gene family.
The type II cytokeratins consist of basic or neutral proteins which are
arranged in pairs of heterotypic keratin chains coexpressed during differentiation
of simple and stratified epithelial tissues.
This type II cytokeratin is specifically expressed in the basal layer of the
epidermis with family member KRT14.
Mutations in these genes have been associated with a complex of diseases
termed epidermolysis bullosa simplex. The type II cytokeratins are clustered in a
region of chromosome 12q12-q13.
control: squamous/stratified squamous
20. CK16 Positive control
Human breast carcinoma tissue and HepG2 cell extracts.
Mouse monoclonal to CK16. Keratin 16 is expressed in keratinocytes,
which are undergoing rapid turnover in the suprabasal region ,also known
as hyperproliferationrelated keratins). Keratin 16 is absent in normal breast
tissue and in noninvasive breast carcinomas. Only 10% of the invasive
breast carcinomas show diffuse or focal positivity. Reportedly, a relatively
high concordance was found between the carcinomas immunostaining
with the basal cell and the hyperproliferationrelated keratins, but not
between these markers and the proliferation marker Ki67. This supports
the conclusion that basal cells in breast cancer may show extensive
proliferation, and that absence of Ki67 staining does not mean that (tumor)
cells are not proliferating.
http://www.biorbyt.com/ck16-antibody-3
human gullet cancer tissue using CK16
antibody
21. CYCLIN D1 antibody
The protein encoded by this gene belongs to the highly conserved cyclin family, whose members are
characterized by a dramatic periodicity in protein abundance throughout the cell cycle.
Cyclins function as regulators of CDK kinases. Different cyclins exhibit distinct expression and degradation
patterns which contribute to the temporal coordination of each mitotic event. This cyclin forms a complex with and
functions as a regulatory subunit of CDK4 or CDK6, whose activity is required for cell cycle G1/S transition.
This protein has been shown to interact with tumor suppressor protein Rb and the expression of this gene is
regulated positively by Rb. Mutations, amplification and overexpression of this gene, which alters cell cycle
progression, are observed frequently in a variety of tumors and may contribute to tumorigenesis.(RefSeqJul2008)
Aliases of CCND1
Cyclin D1
PRAD1 Oncogene
BCL1
Cyclin D1 (PRAD1: Parathyroid Adenomatosis 1)
PRAD1
G1/S-Specific Cyclin D1
D11S287E
Parathyroid Adenomatosis 1
B-Cell CLL/Lymphoma 1
U21B31
B-Cell Lymphoma 1 Protein
G1/S-Specific Cyclin-D1
BCL-1 Oncogene
PRAD1 Oncogene
Immunogen Synthetic peptide corresponding to Human
Cyclin D1 (C terminal).
EpitopeC-terminus
Positive control Breast carcinomas, mantle cell lymphoma,
MCF7 cell lysate
http://www.abcam.com/cyclin-d1-antibody-sp4-ab16663.html#description_images_1
mouse testis tissue, staining Cyclin D1 with ab16663.
http://www.genecards.org/
22. ER
Estrogen Receptor Alpha (ER Alpha) is a nuclear protein and member of the steroid hormone receptor
family. ER alpha possesses both DNA binding and ligand binding domains, and exerts a significant
role in activating the transcription of certain genes. Ligand-dependent dimerization and
phosphorylation both function to regulate the transcriptional activation of ER alpha.
http://www.epitomics.com/diagnostics/product/2156
23. PR
Present in hormone responsive tissue and their neoplasm. also reported in
carcinoma of lung,stomach and thyroid. STUMP (smooth muscle tumor of uncertain malignant
potential )and stromal sarcomas are positive for PR.
Handbook of Practical Immunohistochemistry: Frequently Asked Questions
edited by Fan Lin, Jeffrey Prichard
PR y85
cellmarque.com/antibodies/Progesterone-Receptor-Y85 cellmarque.com/antibodies/Progesterone-Receptor-SP42
PR SP42
24. PR
Formalin-fixed, paraffin-embedded
human breast carcinoma stained with PR
antibody using peroxidase-conjugate and
AEC chromogen. Note nuclear staining of
tumor cells.
https://www.lifetechnologies.com/order/genome-database/antibody/Progesterone-Receptor-Antibody-hPRa-2-Monoclonal/MA5-12642
25. S100
Small dimeric member of the family of calcium-binding proteins.
Widely distributed in human tissues, including glia, neurons,chondrocytes, Schwann
cells,melanocytes,phagocytic or antigen-presenting mononuclear cells.
Langerhans,histiocytes,myoepithelial cells and various epithelia.
http://www.abcam.com/s100-beta-antibody-astrocyte-marker-ab41548.html
ab41548 staining S100 beta in mouse brain tissue sections by Immunohistochemistry (IHC-P -
paraformaldehyde-fixed, paraffin-embedded sections). Tissue was fixed with formaldehyde
and blocked with 1% BSA for 10 minutes; antigen retrieval was by heat mediation in
citric acid. Samples were incubated with primary antibody (1/10000 in TBS/BSA/azide)
for 2 hours at 21°C. A Biotin-conjugated goat anti-rabbit IgG polyclonal (1/250) was
used as the secondary antibody.
At this dilution factor, there is very good delineation of astrocyte processes.
26. p504s
Alpha-methylacyl-CoA racemase (AMACR), also known as p504s, is a mitochondrial and peroxisomal
enzyme that is involved in bile acid biosynthesis and beta-oxidation of branched-chain fatty acids. AMACR is
essential in lipid metabolism, and is expressed in normal liver (hepatocytes), kidney (tubular epithelial cells)
and gallbladder (epithelial cells). Expression has also been found in lung (bronchial epithelial cells) and colon
(colonic surface epithelium). Expression is granular and cytoplasmic. AMACR expression can also be found
in hepatocellular carcinoma and kidney carcinoma. Past studies have also shown that AMACR is expressed
in various colon carcinomas (well, moderately and poorly differentiated) and over expressed in prostate
carcinoma.
Human prostatic adenocarcinoma: immunohistochemical staining for
alpha-methylacyl-CoA racemase (AMACR, p504S) using NCL-L-
AMACR. Paraffin section.
http://www.leicabiosystems.com/ihc-ish-fish/novocastra-reagents/primary-antibodies/details/product/alpha-methylacyl-coa-racemase-amacr-
p504s/
27. TTF-1
This gene encodes a transcription termination factor that is localized to the nucleolus and plays a
critical role in ribosomal gene transcription. The encoded protein mediates the termination of RNA
polymerase I transcription by binding to Sal box terminator elements downstream of pre-rRNA coding
regions. Alternatively spliced transcript variants encoding multiple isoforms have been observed for
this gene. This gene shares the symbol/alias 'TFF1' with another gene, NK2 homeobox 1, also known
as thyroid transcription factor 1, which plays a role in the regulation of thyroid-specific gene
expression. [provided by RefSeq, Apr 2011]
In lung adenocarcinomas, positive and partial positive TTF-1 expression has a
significant positive correlation with EGFR mutations(exon 19 and 21). In clinical
practice, TTF-1 expression combine with EGFR mutations, especially exon 21
mutation can guide clinical treatment timely for lung adenocarcinomas.
Citation: Shanzhi W, Yiping H, Ling H, Jianming Z, Qiang L (2014) The Relationship between
TTF-1 Expression and EGFR Mutations in Lung Adenocarcinomas. PLoS ONE 9(4): e95479.
doi:10.1371/journal.pone.0095479
TTF-1 positive expression in
adenocarcinoma cell (IHC×400).
transcription termination factor, RNA polymerase I
28. MART-1
A tumor-associated melanocytic differentiation antigen. Vaccination with MART-1
antigen may stimulate a host cytotoxic T-cell response against tumor cells
expressing the melanocytic differentiation antigen, resulting in tumor cell lysis.
Synonyms:
Antigen LB39-AA
Antigen SK29-AA
MART-1
MART-1 Tumor Antigen
Melan A
Melan-A Protein
Melanoma Antigen Recognized
by T-Cells 1
MLANA
MLANA Protein
● Commonly used melanocytic markers; MelanA also called A103; are separate antibodies that
occasionally have different staining properties
● Melanocytic Antigen Recognized by cytotoxic T lymphocytes from melanoma patients
● Cytoplasmic protein sensitive and specific for melanoma and melanocytic lesions
Uses by pathologists
=========================================================================
● Recommended for evaluating sentinel lymph nodes for melanoma (Am J Surg Pathol
2001;25:1039), although also stains benign nevi (Am J Surg Pathol 2002;26:1351) and normal
melanocytes
● Differentiate adrenal cortical tumors (MART1+) vs. renal cell carcinoma or pheochromocytoma
(MART1-)
● Differentiate neurotized melanocytic nevi (MelanA+) from neurofibroma (MelanA-, Arch Pathol
Lab Med 2012;136:810)
● Distinguish in situ and invasive melanoma, and measure thickness (Am J Dermatopathol
2012 Jun 8 [Epub ahead of print])
● Caution: may overestimate presence of lentigo maligna (Dermatol Surg 2011;37:657, J
Cutan Pathol 2011;38:775)
29. MART-1 mRNA (blue/purple color) is seen by RT in situ PCR
in melanophages with coarse pigment granules (Panels A&B).
Immunohistochemistry for MART-1 shows a weakly positive
signal in scattered large cells with “normal” nuclei and coarse
melanin granules, consistent with melanophages (Panel C).
Immunohistochemistry for HMB-45 shows a positive signal in
scattered large cells, consistent with melanophages (Panel D).
Double staining of MART-1 mRNA (blue/purple color) and
CD68 antigen (red color) shows that some cells co-express
both MART-1 mRNA and CD68 (arrow), while MART-1
mRNA and CD68 are separately expressed by other cells.
(Panels E&F). Sentinel node (Panel G) and NSN (Panel H)
from a breast cancer patient are negative for MART-1 mRNA.
Am J Surg Pathol. Author manuscript; available in PMC 2012 Nov 1.
Am J Surg Pathol. 2011 Nov; 35(11): 1657–1665.
doi: 10.1097/PAS.0b013e3182322cf7
30. KAPPA/LAMBDAImmunohistochemical staining for kappa and lambda light chains is often performed on lymphoid tissue. Staining
for kappa and lambda light chain expression is notoriously problematic—some might say finicky. One complication
is the need for decalcification on some lymphoid tissue often stained for kappa and lambda, such as bone marrow
core biopsies. The more common fixatives currently in use have different effects on the various tissues under
study and may impart different properties to the protein targets in question.
Anti-kappa and anti-lambda detect surface light chain immunoglobulins on normal and neoplastic B-cells in
human lymphoid tissue. In normal lymphoid tissue the kappa and lambda cell ratio is approximately 2:1,
but values in excess of that ratio indicate monoclonality caused by either a lymphoproliferative disorder or
neoplasia such as lymphoma.
Both kappa (M) (brown) and lambda (P) (red) seen
on the same tissue section, thus allowing the end-
user a more accurate and easier assessment
of both stains. Image analysis of a digitally scanned
slide provides rapid highly accurate kappa and
lambda cell counts. The resulting whole slide section
determination of a kappa/lambda ratio enables easier
diagnosis of disease.
http://flagshipbio.com/lymph/kappalambda-in-lymphoma/
