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Product Info

Source:
Mouse
Application:
ELISA 1:10000, WB 1:500-1:2000
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human
Clonality:
Monoclonal [AFB1480]
Specificity:
human Albumin antibody detects endogenous levels of total human Albumin.
RRID:
AB_2833505
Cite Format: Affinity Biosciences Cat# BF0544, RRID:AB_2833505.
Conjugate:
Unconjugated.
Purification:
Affinity-chromatography.
Storage:
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

alb; ALBU_HUMAN; Albumin (32 AA); Albumin (AA 34); Albumin; Analbuminemia; Bisalbuminemia; Cell growth inhibiting protein 42; DKFZp779N1935; Dysalbuminemic hyperthyroxinemia; Growth inhibiting protein 20; HSA; Hyperthyroxinemia dysalbuminemic; PRO0883; PRO0903; PRO1341; Serum albumin;

Immunogens

Immunogen:

Purified recombinant fragment of human human Albumin expressed in E. Coli.

Uniprot:
Gene(ID):
Expression:
Description:
Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Albumin is a globular unglycosylated serum protein of molecular weight 65,000. Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin.
Sequence:
MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL

PTMs - P02768 As Substrate

Site PTM Type Enzyme
S14 Phosphorylation
Y17 Phosphorylation
S18 Phosphorylation
S29 Phosphorylation
K44 Acetylation
Y54 Phosphorylation
C58 S-Nitrosylation
K65 Acetylation
T71 Phosphorylation
K75 Acetylation
K75 Methylation
C77 S-Nitrosylation
S82 Phosphorylation
C86 S-Nitrosylation
S89 Phosphorylation
T92 Phosphorylation
C99 S-Nitrosylation
T107 Phosphorylation
Y108 Phosphorylation
C114 S-Nitrosylation
C115 S-Nitrosylation
K117 Acetylation
C125 S-Nitrosylation
K130 Acetylation
C148 S-Nitrosylation
K160 Acetylation
K161 Acetylation
Y162 Phosphorylation
Y164 Phosphorylation
R168 Methylation
Y172 Phosphorylation
Y174 Phosphorylation
K183 Acetylation
K186 Acetylation
T190 Phosphorylation
C192 S-Nitrosylation
C193 S-Nitrosylation
K198 Acetylation
C201 S-Nitrosylation
K214 Acetylation
S216 Phosphorylation
S217 Phosphorylation
K219 Acetylation
K223 Acetylation
K229 Acetylation
K229 Ubiquitination
S244 Phosphorylation
K249 Acetylation
S256 Phosphorylation
K257 Acetylation
T260 Phosphorylation
T263 Phosphorylation
K264 Acetylation
C269 S-Nitrosylation
C270 S-Nitrosylation
K286 Acetylation
Y287 Phosphorylation
C289 S-Nitrosylation
S294 Phosphorylation
S296 Phosphorylation
S297 Phosphorylation
K298 Acetylation
K298 Ubiquitination
K300 Acetylation
C303 S-Nitrosylation
K305 Acetylation
S311 Phosphorylation
C313 S-Nitrosylation
S328 Phosphorylation
S336 Phosphorylation
Y343 Phosphorylation
K347 Acetylation
Y365 Phosphorylation
S366 Phosphorylation
T376 Phosphorylation
Y377 Phosphorylation
T379 Phosphorylation
T380 Phosphorylation
C385 S-Nitrosylation
Y394 Phosphorylation
K396 Acetylation
K402 Acetylation
C416 S-Nitrosylation
Y425 Phosphorylation
K426 Acetylation
T436 Phosphorylation
K438 Acetylation
S443 Phosphorylation
T444 O-Glycosylation
T444 Phosphorylation
T446 Phosphorylation
S451 Phosphorylation
K456 Acetylation
K468 Acetylation
C472 S-Nitrosylation
Y476 Phosphorylation
C485 S-Nitrosylation
K490 Methylation
T498 Phosphorylation
K499 Acetylation
C500 S-Nitrosylation
T502 Phosphorylation
S504 Phosphorylation
C511 S-Nitrosylation
S513 Phosphorylation
T520 Phosphorylation
Y521 Phosphorylation
K524 Acetylation
C538 S-Nitrosylation
K549 Acetylation
T551 Phosphorylation
K558 Acetylation
K558 Methylation
K562 Acetylation
T564 Phosphorylation
T590 Phosphorylation
C591 S-Nitrosylation
K597 Acetylation
K598 Acetylation
S603 Phosphorylation

Research Backgrounds

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 (Probable). Its main function is the regulation of the colloidal osmotic pressure of blood (Probable). Major zinc transporter in plasma, typically binds about 80% of all plasma zinc. Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli. Does not prevent iron uptake by the bacterial siderophore aerobactin.

PTMs:

Kenitra 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.

Phosphorylated by FAM20C in the extracellular medium.

Acetylated on Lys-223 by acetylsalicylic acid.

Subcellular Location:

Secreted.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Plasma.

Subunit Structure:

Interacts with FCGRT; this interaction regulates ALB homeostasis.

Family&Domains:

Belongs to the ALB/AFP/VDB family.

Research Fields

· Organismal Systems > Endocrine system > Thyroid hormone synthesis.

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