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Gamma-crystallin A Antibodies

AND CRYGA ELISA kits, Gamma-crystallin A Proteins

Many biological assays use antibodies to detect Gamma-crystallin A, such as Western Blot (WB), ELISA, Flow Cytometry, Immunocytochemistry (IHC). These antibodies can be polyclonal or monoclonal, and react with Gamma-crystallin A in Human, Mouse, Rat, and many other animal samples. Boster Bio use mainly mouse and rabbit to develop Gamma-crystallin A antibodies...

We validate the specificity of these antibodies to Gamma-crystallin A by testing them on tissues known to express CRYGA positively and negatively. Browse below to find the CRYGA antibody that suites your experiment. We have 1 of these antibodies and many publications and validation images.

If you cannot find antibodies that fit your needs, contact us for making custom antibodies. We have a full suite of custom antibody services covering from research to diagnostic and therapeutic applications.

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CRYGA Infographic by Boster Bio

CRYGA protein infographic

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CRYGA (NM_014617) Human Over-expression Lysate

CRYGA Human Over-expression Lysates NM_014617

CRYGA Human Over-expression Lysates NM_014617

Human

$628
Cat # LS001418
20 µg, 100 µg

CRYGA Overview

Facts about Gamma-crystallin A.

CRYGA 3D structure

CRYGA 3D structure. Source: alphafold

Gamma-crystallin A (CRYGA)

Crystallins are the dominant structural components of the vertebrate eye lens. .

Gene Information

Human
Gene Name:	CRYGA
Uniprot:	P11844
Entrez:	1418

Gene Information

Family

Belongs to:

beta/gamma-crystallin family

Family

Alternative Names

Gamma-crystallin A

Molecular Weight

Mass (kDA):
20.877 kDA

Molecular Weight

Genomic Context


Human

Location:	2q33.3
Sequence:	2; NC_000002.12 (208160740..208163589, complement)

Bosterbio | ELISA Kits, Antibodies, Antibody Company

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/CRYGA

References

PMID: 3670288 by Meakin S.O., et al. Gamma-crystallins of the human eye lens: expression analysis of five members of the gene family.

PMID: 12507494 by Salim A., et al. Homology models of human gamma-crystallins: structural study of the extensive charge network in gamma-crystallins.