Native Mouse Albumin protein (Azide free) (ab183228)
Key features and details
- Expression system: Native
- Purity: > 95% SDS-PAGE
- Suitable for: SDS-PAGE
-
Product name
Native Mouse Albumin protein (Azide free)
See all Albumin proteins and peptides -
Purity
> 95 % SDS-PAGE. -
Expression system
Native -
Accession
-
Protein length
Full length protein -
Animal free
No -
Nature
Native -
-
Species
Mouse -
Sequence
EAHKSEIAHRYNDLGEQHFKGLVLIAFSQYLQKCSYDEHAKLVQEVTDFA KTCVADESAANCDKSLHTLFGDKLCAIPNLRENYGELADCCTKQEPERNE CFLQHKDDNPSLPPFERPEAEAMCTSFKENPTTFMGHYLHEVARRHPYFY APELLYYAEQYNEILTQCCAEADKESCLTPKLDGVKEKALVSSVRQRMKC SSMQKFGERAFKAWAVARLSQTFPNADFAEITKLATDLTKVNKECCHGDL LECADDRAELAKYMCENQATISSKLQTCCDKPLLKKAHCLSEVEHDTMPA DLPAIAADFVEDQEVCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLA KKYEATLEKCCAEANPPACYGTVLAEFQPLVEEPKNLVKTNCDLYEKLGE YGFQNAILVRYTQKAPQVSTPTLVEAARNLGRVGTKCCTLPEDQRLPCVE DYLSAILNRVCLLHEKTPVSEHVTKCCSGSLVERRPCFSALTVDETYVPK EFKAETFTFHSDICTLPEKEKQIKKQTALAELVKHKPKATAEQLKTVMDD FAQFLDTCCKAADKDTCFSTEGPNLVTRCKDALA -
Predicted molecular weight
66 kDa -
Amino acids
25 to 608 -
Additional sequence information
Purified from Mouse plasma.
-
Preparation and Storage
-
Alternative names
- alb
- ALBU_HUMAN
- Albumin (32 AA)
see all -
Function
Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc. -
Tissue specificity
Plasma. -
Involvement in disease
Defects in ALB are a cause of familial dysalbuminemic hyperthyroxinemia (FDH) [MIM:103600]. FDH is a form of euthyroid hyperthyroxinemia that is due to increased affinity of ALB for T(4). It is the most common cause of inherited euthyroid hyperthyroxinemia in Caucasian population. -
Sequence similarities
Belongs to the ALB/AFP/VDB family.
Contains 3 albumin domains. -
Post-translational
modificationsKenitra variant is partially O-glycosylated at Thr-620. It has two new disulfide bonds Cys-600 to Cys-602 and Cys-601 to Cys-606.
Glycated in diabetic patients.
Phosphorylation sites are present in the extracelllular medium.
Acetylated on Lys-223 by acetylsalicylic acid. -
Cellular localization
Secreted. - Information by UniProt
