CD14, Monoclonal Antibody

Mouse Anti-Human CD14 - Purified, Unlabeled Antibody; Mouse Anti-Human CD14

For Research Use Only. Not for use in diagnostic procedures.

Chromosome: 5; NC_000005.9 (140024948..140027370, complement). Location: 5q31.2

Monoclonal

Mouse IgG1

61D3

Mouse

Human CD14
CD14 is a 53-55 kDa glycosphosphatidylinositol (GPI)-anchored single chain glycoprotein. It is expressed on monocytes, macrophages, dendritic cells and Langerhans cells. It is also weakly expressed on neutrophils. CD14 appears to be involved in clearance of gram-negative bacteria via its high affinity binding to LPS-LPB complexes.1-4

Purified (UNLB) Antibody

The purified (UNLB) antibody is supplied as 0.1 mg of purified immunoglobulin in 1.0 mL of 100 mM borate buffered saline, pH 8.2. No preservatives or amine-containing buffer salts added. Store at 2- 8 degree C.
The fluorescein (FITC), Alexa Fluor 488 (AF488), and Alexa Fluor 647 (AF647) conjugates are supplied as 100 tests in 1.0 mL of PBS/NaN3. Store at 2-8 degree C.
The biotin (BIOT) conjugate is supplied as 100 tests in 1.0 mL PBS/NaN3. Store at 2-8 degree C.
The R-PE conjugate and allophycocyanin conjugates are supplied as 100 tests in 1.0 mL of PBS/NaN3 and a stabilizing agent; store at 2-8 degree C.
The low endotoxin/azide-free antibody is supplied as 0.1 mg purified immunoglobulin in 0.2 mL of PBS; aliquot and freeze upon receipt.
The Spectral Red (SPRD), R-phycoerythrin-Cyanine 5.5 (R-PE-CY 5.5), R-phycoerythrin-Cyanine 7 (R-PE-CY 7), Allophycocyanin-Cyanine 5.5 (APC-CY 5.5), and Allophycocyanin-Cyanine 7 (APCCY 7) conjugates are supplied as 100 tests in 1.0 mL of PBS/NaN3 and a stabilizing agent. Store at 2-8 degree C. Do not freeze!
Protect conjugated forms from light. Reagents are stable for the period shown on the label if stored as directed.

Small volumes of anti-NDUFA2 antibody 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.

Flow Cytometry; Immunohistochemistry (Frozen Sections); Immunoprecipitation

Flow Cytometry Suggested Dilution: <= 1 ug/10^6 cells

10,922 Da[Similar Products]

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, 2, 8kDa

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2; NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2; OTTHUMP00000159890; OTTHUMP00000223709; complex I B8 subunit; NADH-ubiquinone oxidoreductase subunit CI-B8

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2

NDUA2_HUMAN

The encoded protein is a subunit of the hydrophobic protein fraction of the NADH:ubiquinone oxidoreductase (complex 1), the first enzyme complex in the electron transport chain located in the inner mitochondrial membrane, and may be involved in regulating complex I activity or its assembly via assistance in redox processes. Mutations in this gene are associated with Leigh syndrome, an early-onset progressive neurodegenerative disorder. Alternative splicing results in multiple transcript variants.

Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.

Subunit structure: Complex I is composed of 45 different subunits.

Subcellular location: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.

1. Knapp, W., B. Dorken, W.R. GIlks, E.P. Rieber, R.E. Schmidt, H. Stein, A.E.G.K. Von dem Borne, eds. 1989. Leukocyte Typing IV: White Cell Differentiation Antigens, Oxford University Press, Oxford.
2. Barclay, A.N., M.H. Brown, S.K.A. Law, A.J. McKnight, M.G. Tomlinson, and P.A. van der Merwe, eds. 1997. The Leukocyte Antigens Facts Book, 2nd Edition, CD14 Section, Academic Press, New York, p. 169.
3. Hogg, N., S. MacDonald, M. Slusarenko, and P.C. Beverley. 1984. Immunol. 53:753.
4. Stocks, S.C., M. Albrechtsen, and M.A. Kerr. 1990. Biochem. J. 268:275.

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