HSPB8 (Alpha Crystallin C Chain, Alpha-Crystallin C Chain, Charcot Marie Tooth Disease axonal Type 2L, Charcot Marie Tooth Disease spinal, CMT2L, CRYAC, DHMN 2, DHMN2, E2 induced Gene 1 Protein, E2-induced Gene 1 Protein, E2IG1, H11, Heat Shock 22kDa Protein 8, Heat Shock 27kDa Protein 8, Heat Shock Protein 22, Heat Shock Protein beta 8, Heat Shock Protein beta-8, Hereditary motor neuropathy distal, HMN 2, HMN2, HMN2A, HSB8, HSPB 8, Hspb8, HSPB8_HUMAN, OTTHUMP00000239768, Protein Kinase H11, Small stress Protein like Protein HSP22, Small stress Protein-like Protein HSP22, Spinal muscular atrophy distal adult autosomal dominant)
Référence 223431-50ul
Conditionnement : 50ul
Marque : US Biological
223431 HSPB8 (Alpha Crystallin C Chain, Alpha-Crystallin C Chain, Charcot Marie Tooth Disease axonal Type 2L, Charcot Marie Tooth Disease spinal, CMT2L, CRYAC, DHMN 2, DHMN2, E2 induced Gene 1 Protein, E2-induced Gene 1 Protein, E2IG1, H11, Heat Shock 22kDa Protein 8, Heat Shock 27kDa Protein 8, Heat Shock Protein 22, Heat Shock Protein beta 8, Heat Shock Protein beta-8, Hereditary motor neuropathy distal, HMN 2, HMN2, HMN2A, HSB8, HSPB 8, Hspb8, HSPB8_HUMAN, OTTHUMP00000239768, Protein Kinase H11, Small stress Protein like Protein HSP22, Small stress Protein-like Protein HSP22, Spinal muscular atrophy distal adult autosomal dominant)
Clone Type
PolyclonalHost
rabbitSource
humanSwiss Prot
Q9UJY1Isotype
IgGGrade
Affinity PurifiedApplications
IHC WBCrossreactivity
Hu Mo RtShipping Temp
Blue IceStorage Temp
-20°CCrystallins are the major proteins expressed in the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into a, b and g families; b and g-crystallins compose a superfamily. Crystallins usually contain seven distinctive protein regions, including four homologous motifs, a connecting peptide, and N- and C-terminal extensions. a-crystallins consist of three gene products, aA, aB and aC-crystallin, which are members of the small heat shock protein family (HSP20). They are induced by heat shock, and act as molecular chaperones by holding denatured proteins in large soluble aggregates. However, unlike other molecular chaperones, a-crystallins do not renature these proteins. Research indicates that binding occurs between membranes and aC-crystallin. The binding site appears to be at the polar-apolar interface in membrane protein (MIP26) and aC-crystallin; the lipid bilayer becomes less mobile with aC-crystallin binding.||Applications: |Suitable for use in Western Blot, Immunohistochemistry. Other applications not tested.||Recommended Dilution:|Western Blot: 1:500-1:2000|Immunohistochemistry: 1:50-1:200|Optimal dilutions to be determined by the researcher.||Storage and Stability:|May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.