Recombinant Mouse Relaxin-1 Protein

Catalog #: 6637-RN Datasheet / COA / SDS

Carrier Free

Catalog #	Availability	Size / Price	Qty
6637-RN-025/CF

With Carrier

Catalog #	Availability	Size / Price	Qty
6637-RN-025

R&D Systems Recombinant Proteins and Enzymes

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Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Mouse Relaxin-1 Protein Summary

Product Specifications

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

Activity

Measured by its ability to induce cAMP accumulation in THP‑1 human acute monocytic leukemia cells. Parsell, D.A. et al. (1996) J. Biol. Chem. 271:27936.

The ED₅₀ for this effect is 2-8 ng/mL.

Source

E. coli-derived mouse Relaxin-1 protein
Arg23-Arg54, with an N-terminal Met (B chain) & Glu161-Cys185 (A chain)

Accession #

NP_035402

N-terminal Sequence
Analysis

Met (B chain) & Glu161 (A chain)

Structure / Form

Disulfide-linked heterodimer

Predicted Molecular Mass

3.9 kDa (B chain) & 2.7 kDa (A chain)

SDS-PAGE

4 & 3 kDa, reducing conditions

Product Datasheets

6637-RN (with carrier)

Product Datasheet

COA

SDS

6637-RN/CF (carrier free)

Product Datasheet

COA

SDS

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

6637-RN

Formulation	Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Reconstitution	Reconstitute at 100 μg/mL in PBS containing at least 0.1% human or bovine serum albumin.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:	Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 °C as supplied. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 to -70 °C under sterile conditions after reconstitution.

6637-RN/CF

Formulation	Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution	Reconstitute at 100 μg/mL in PBS.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:	Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 °C as supplied. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Reconstitution Calculator

Background: Relaxin-1

Mouse Relaxin-1 (RLN1 or M1 relaxin) is the counterpart of human relaxin-2 (H2 relaxin) within the structurally related insulin/relaxin superfamily, while orthologs of the human relaxin-1 are found only in higher primates (1, 2). As with other insulin/relaxin superfamily members, RLN1 is synthesized as a preprohormone (1 ‑ 3, 5). Processing of the 21 kDa preprorelaxin-1 includes removal of the signal sequence, formation of two disulfide bonds between A and B chains and removal of the intervening C‑chain by a prohormone convertase. The resulting mature protein is an unglycosylated 6 kDa dimer of disulfide-linked A and B chains that binds the leucine-rich G-protein coupled receptor RXFP1, previously called LGR7 (1 ‑ 4). Mouse RLN1 shares only 67%, 39%, 36% and 42% amino acid (aa) identity with rat, equine and feline RLN1 and human Relaxin-2, respectively, and its activity shows partial species specificity. For example, a unique amino acid near the end of the A chain in mice, Tyr184, lowers its affinity for RXFP1 compared to other species (5). Mouse RLN1 is prominently expressed in the prostate and ovary, with lower levels in the brain, heart and other organs (1 ‑ 3). In the prostate, RLN1 is anti-apoptotic and contributes to development and maintenance of male fertility (6). In the female mouse, circulating RLN1 produced by the corpus luteum during pregnancy is essential for growth and softening of the cervix and vagina in preparation for delivery. It also promotes development of the mouse mammary apparatus, regulates plasma osmolality, and increases cardiac output and glomerular filtration rate in pregnancy (1, 2). Many RLN1 effects on reproductive tissues are augmented by estrogen (1 ‑ 3, 7). In non‑reproductive tissues, RLN1 mediates collagen turnover (7). RLN1-deficient mice develop age‑related fibrosis and smooth muscle hypertrophy in organs such as lung, heart, kidney and liver (7 ‑ 10).

References