SLC11A1 Antibody | 63-497

SLC11A1 Antibody | 63-497 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Human

Homology: N/A

Immunogen: This SLC11A1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 250-276 amino acids from the Central region of human SLC11A1.

Research Area: Immunology, Obesity, Signal Transduction

Tested Application: WB, IF

Application: For WB starting dilution is: 1:1000

Specificiy: N/A

Positive Control 1: N/A

Positive Control 2: N/A

Positive Control 3: N/A

Positive Control 4: N/A

Positive Control 5: N/A

Positive Control 6: N/A

Molecular Weight: 60 kDa

Validation: N/A

Isoform: N/A

Purification: This antibody is purified through a protein A column, followed by peptide affinity purification.

Clonality: Polyclonal

Clone: N/A

Isotype: Rabbit Ig

Conjugate: Unconjugated

Physical State: Liquid

Buffer: Supplied in PBS with 0.09% (W/V) sodium azide.

Concentration: batch dependent

Storage Condition: Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.

Alternate Name: Natural resistance-associated macrophage protein 1, NRAMP 1, Solute carrier family 11 member 1, SLC11A1, LSH, NRAMP, NRAMP1

User Note: Optimal dilutions for each application to be determined by the researcher.

BACKGROUND: NRAMP1, also known as SLC11A1, is a member of the solute carrier family 11 (proton-coupled divalent metal ion transporters) family and encodes a multi-pass membrane protein. The protein functions as a divalent transition metal (iron and manganese) transporter involved in iron metabolism and host resistance to certain pathogens. Mutations in this gene have been associated with susceptibility to infectious diseases such as leprosy and tuberculosis, and inflammatory diseases such as Crohn disease and rheumatoid arthritis. Alternatively spliced variants that encode different protein isoforms have been described but the full-length nature of only one has been determined.