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CRYAB recombinant protein :: Alpha-crystallin B chain (CRYAB) Recombinant Protein

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Catalog # MBS966062
Unit / Price
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  0.05 mg (E-Coli)  /  $575 +1 FREE 8GB USB
  0.05 mg (Yeast)  /  $705 +1 FREE 8GB USB
  0.2 mg (E-Coli)  /  $765 +1 FREE 8GB USB
  0.5 mg (E-Coli)  /  $845 +1 FREE 8GB USB
  0.05 mg (Baculovirus)  /  $945 +1 FREE 8GB USB
  0.2 mg (Yeast)  /  $965 +1 FREE 8GB USB
  0.5 mg (Yeast)  /  $1,085 +1 FREE 8GB USB
  0.05 mg (Mammalian-Cell)  /  $1,180 +1 FREE 8GB USB
  1 mg (E-Coli)  /  $1,265 +1 FREE 8GB USB
  0.1 mg (Baculovirus)  /  $1,355 +1 FREE 8GB USB
  1 mg (Yeast)  /  $1,720 +2 FREE 8GB USB
  0.5 mg (Baculovirus)  /  $1,780 +2 FREE 8GB USB
  0.1 mg (Mammalian-Cell)  /  $1,925 +2 FREE 8GB USB
  1 mg (Baculovirus)  /  $2,765 +3 FREE 8GB USB
CRYAB recombinant protein
Product Name

Alpha-crystallin B chain (CRYAB), Recombinant Protein

Full Product Name

Recombinant Rabbit Alpha-crystallin B chain (CRYAB)

Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence Positions
1-175aa, Full length protein
Sequence
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSW IDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK QAPGPERTIP ITREEKPAVT AAPKK
3D Structure
ModBase 3D Structure for P41316
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Purity/Purification
>85% (SDS-PAGE) (lot specific)
Form/Format
Liquid containing glycerol
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
Species
Rabbit
Storage Buffer
Tris-based buffer, 50% glycerol
Preparation and Storage
Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.
ISO Certification
Manufactured in an ISO 13485:2003 and EN ISO 13485:2012 Certified Laboratory.
Other Notes
Small volumes of CRYAB recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
CRYAB recombinant protein
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy.
NCBI/Uniprot data below describe general gene information for CRYAB. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Related Accession #
Molecular Weight
20,107 Da
NCBI Official Full Name
alpha-crystallin B chain
NCBI Official Symbol
CRYAB  [Similar Products]
NCBI Protein Information
alpha-crystallin B chain
UniProt Protein Name
Alpha-crystallin B chain
UniProt Synonym Protein Names
Alpha(B)-crystallin
Protein Family
UniProt Gene Name
CRYAB  [Similar Products]
UniProt Comments for CRYAB
May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.
Precautions
All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.
Disclaimer
While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.
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