Search: 1000 results found for "chromogranin"

Description:

HCC-1 Human Recombinant (CCL14)

Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.

Product # :

CHM-311

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Description

HCC-1 Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 72 amino acids and having a molecular mass of 8411 Dalton. The HCC-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CCL14 protein was lyophilized with 20mM PBS pH-7.4 and 150mM NaCl.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The Biological activity is calculated by its ability to chemoattract Human monocytes at 5-20ng/ml corresponding to a Specific Activity of 50,000-200,000IU/mg.

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Introduction
Chemokine (C-C motif) ligand 14 (CCL14) is a small cytokine belonging to the CC chemokine family. It is also commonly known as HCC-1. It is produced as a protein precursor that is procesed to generate a mature active protein containing 74 amino acids that and is 46% identical in amino acid composition to CCL3 and CCL4. This chemokine is expressed in various tissues including spleen, bone marrow, liver, muscle, and gut. CCL13 activates monocytes, but does not induce their chemotaxis. Human CCL13 is located on chromosome 17 within a cluster of other chemokines belonging to the CC family.
Synonyms
Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized HCC1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL14 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized HCC-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TESSSRGPYHPSECCFTYTTYKIPRQRIMDYYETNSQCSKPGIVFITKRGHS
VCTNPSDKWVQDYIKDMKEN.
Background
What is the molecular weight/Mw of CCL14 HUMAN Protein?
CCL14 HUMAN Protein has a total Mw of 8.41kDa.

What is the source or expression system of CCL14 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL14 HUMAN Protein?
CCL14 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL14 HUMAN Protein?
The Biological activity is calculated by its ability to chemoattract Human monocytes at 5-20ng/ml corresponding to a Specific Activity of 50,000-200,000IU/mg.

What is the amino acid sequence of CCL14 HUMAN Protein?
TESSSRGPYHPSECCFTYTTYKIPRQRIMDYYETNSQCSKPGIVFITKRGHS
VCTNPSDKWVQDYIKDMKEN.

What applications can CCL14 HUMAN Protein be used in?
CCL14 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL14 HUMAN Protein?
The endotoxin level is minimal, CCL14 HUMAN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Cystatin-A Human Recombinant, Active

Cystatin-A, Cystatin-AS, Stefin-A, CSTA, STF1, STFA.

Product # :

PRO-086

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Description

Cystatin A Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 118 amino acids (1-98a.a.) and having a molecular mass of 13.1 kDa.The Cystatin A is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Cystatin-A (1mg/ml) in 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 10% glycerol.

Purity

Greater than 95% as determined by reducing SDS-PAGE.

Biological Activity

The IC50 value is < 1.0nM. The inhibitory function of CSTA on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25C.

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Introduction
Human Cystatin A (CSTA or Stefin A) belongs to family 1 of the cystatin superfamily, which is characterized by the lack of disulphide bonds and carbohydrates. CSTA is an intracellular inhibitor regulating the activities of cysteine proteases of the papain family such as Cathepsins B, H and L. Cystatin A has also been implicated in several disease states. Because of altered proteolytic state in cancer progression, CSTA may have a role in the proteolitic pathways.
Synonyms
Cystatin-A, Cystatin-AS, Stefin-A, CSTA, STF1, STFA.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MIPGGLSEAK PATPEIQEIV DKVKPQLEEK TNETYGKLEA VQYKTQVVAG TNYYIKVRAG DNKYMHLKVF KSLPGQNEDL VLTGYQVDKN KDDELTGF.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

CTACK Mouse Recombinant (CCL27)

C-C motif chemokine 27, CC chemokine ILC, Cutaneous T-cell-attracting chemokine, CTACK, ESkine, IL-11 R-alpha-locus chemokine, ALP, mILC, Skinkine, Small-inducible cytokine A27, Ccl27, Ilc, Scya27.

Product # :

CHM-013

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Description

CTACK Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 95 amino acids and having a molecular mass of 10.9kDa. The CTACK is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH7.4 and 300mM NaCl.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml.

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Introduction
CTACK is a chemotactic factor that attracts skin-associated memory T-lymphocytes. CTACK is involved in mediating homing of lymphocytes to cutaneous sites. CTACK Binds to CCR10.
Synonyms
C-C motif chemokine 27, CC chemokine ILC, Cutaneous T-cell-attracting chemokine, CTACK, ESkine, IL-11 R-alpha-locus chemokine, ALP, mILC, Skinkine, Small-inducible cytokine A27, Ccl27, Ilc, Scya27.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CTACK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTACK should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized CTACK in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN.
Background
What is the molecular weight/Mw of CTACK MOUSE Protein?
CTACK MOUSE Protein has a total Mw of 10.9kDa.

What is the source or expression system of CTACK MOUSE Protein?
Escherichia Coli.

What is the Purity of CTACK MOUSE Protein?
CTACK MOUSE Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of CTACK MOUSE Protein?
The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml.

What is the amino acid sequence of CTACK MOUSE Protein?
LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN.

What applications can CTACK MOUSE Protein be used in?
CTACK MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CTACK MOUSE Protein?
The endotoxin level is minimal, CTACK MOUSE Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

VEGF Co-regulated Chemokine 1 Rat Recombinant

Protein Cxcl17, Cxcl17, RGD1304717, C-X-C motif chemokine 17, VEGF co-regulated chemokine 1, Vcc1, VCC-1.

Product # :

CHM-281

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Description

CXCL17 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 97 amino acids and having a molecular mass of 11.5kDa.The CXCL17 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CXCL17 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, 300mM NaCl, pH 7.4.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Measured by its ability to induce VEGF expression in mouse endothelial cells. The ED₅₀ for this effect is typically 1-5 µg/ml.

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Introduction
Dendritic cell and monocyte chemokinelike protein (DMC/CXCL17/VEGF-correlated chemokine 1/VCC1), is a secreted molecule with a size and predicted 3-dimensional folding pattern similar to that of chemokines CXCL8/IL8 and CXCL14/BRAK. CXCL17 is constitutively generated by airway and intestinal epithelium. CXCL17 induces the chemotaxis of quiescent, but not LPS-activated peripheral blood monocytes and dendritic cells, and it also binds these cells specifically. The expression of CXCL17 is increased in endothelial cells when they are induced to form tubes in vitro. CXCL17, CXCL1/GRO and CXCL8/IL8 which have roles in angiogenesis, show significantly correlated expression with that of VEGF in primary lung, breast and esophageal tumors. Therefore, CXCL17 is suggested to have a role in tumor angiogenesis. The mature Rat CXCL17 shares 82%, 71% amino acid sequence identity with mouse, human CXCL17, respectively.
Synonyms
Protein Cxcl17, Cxcl17, RGD1304717, C-X-C motif chemokine 17, VEGF co-regulated chemokine 1, Vcc1, VCC-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CXCL17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL17 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized CXCL17 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SPNQEVARHH GDQHQAPRRW LWEGGQECDC KDWSLRVSKR KTTAVLEPPR KQCPCDHVKG SEKKNRRQKH HRKSQRPSRT CQQFLKRCQL ASFTLPL.
Background
What is the molecular weight/Mw of CXCL17 RAT Protein?
CXCL17 RAT Protein has a total Mw of 11.5kDa.

What is the source or expression system of CXCL17 RAT Protein?
Escherichia Coli.

What is the Purity of CXCL17 RAT Protein?
CXCL17 RAT Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL17 RAT Protein?
Measured by its ability to induce VEGF expression in mouse endothelial cells. The ED50 for this effect is typically 1-5 µg/ml.

What is the amino acid sequence of CXCL17 RAT Protein?
SPNQEVARHH GDQHQAPRRW LWEGGQECDC KDWSLRVSKR KTTAVLEPPR KQCPCDHVKG SEKKNRRQKH HRKSQRPSRT CQQFLKRCQL ASFTLPL.

What applications can CXCL17 RAT Protein be used in?
CXCL17 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL17 RAT Protein?
The endotoxin level is minimal, CXCL17 RAT Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Osteocrin Human Recombinant

Osteocrin, Musclin, OSTN.

Product # :

PRO-420

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Description

The recombinant Human Osteocrin is produced with N-terminal fusion of His Tag. The Human Osteocrin His-Tagged Fusion Protein is 13.6 kDa containing 106 amino acid residues of the human Osteocrin and 16 additional amino acid residues – His Tag (underlined).

Source

Escherichia Coli.

Formulation

Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer, pH 4.0.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Osteocrin is a recently identified secreted protein expression of which was only detected in bone, peaking just after birth and decreasing markedly with age. A 1280-bp mRNA encodes osteocrin producing a mature protein of 103 amino acids with a molecular mass of 11.4 kDa. In primary osteoblastic cell cultures osteocrin expression coincided with matrix formation then decreased in very mature cultures. Treatment of cultures with 1,25-dihydroxyvitamin D3 resulted in a rapid dose- dependent down-regulation of osteocrin expression, suggesting direct regulation. Chronic treatment of primary cultures with osteocrin-conditioned media inhibited mineralization and reduced osteocalcin and alkaline phosphatase expression. These results suggest that osteocrin represents a novel, unique vitamin D-regulated bone-specific protein that appears to act as a soluble osteoblast regulator.
Synonyms
Osteocrin, Musclin, OSTN.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MRGSHHHHHH GMASHMVDVT TTEAFDSGVI DVQSTPTVRE EKSATDLTAK LLLLDELVSL ENDVIETKKK RSFSGFGSPL DRLSAGSVDH KGKQRKVVDH PKRRFGIPMD RIGRNRLSNS RG.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Exodus-2 Mouse Recombinant (CCL21)

Small inducible cytokine A21, CCL21, Beta chemokine exodus-2, 6Ckine, Secondary lymphoid-tissue chemokine, SLC, chemokine (C-C motif) ligand 21, ECL, CKb9, TCA4, SCYA21, MGC34555.

Product # :

CHM-371

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Description

Exodus-2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 110 amino acids and having a molecular mass of 12kDa. The CCL21 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM Phosphate buffer and 0.15M NaCl pH-7.4.

Purity

Greater than 97.0% as determined by SDS-PAGE & RP-HPLC.

Biological Activity

Determined by its ability to chemoattract total murine T cell population using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

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Introduction
Chemokine (C-C motif) ligand 21 (CCL21) is a small cytokine belonging to the CC chemokine family. This chemokine is also known as 6Ckine (because it has six conserved cysteine residues instead of the four cysteines typical to chemokines), exodus-2, and secondary lymphoid-tissue chemokine (SLC). CCL21 is expressed predominantly in the lymph nodes and, in contrast to other CC chemokines, is chemotactic for lymphocytes. The gene for CCL21 is located on human chromosome 9. CCL21 elicits its effects by binding to a cell surface chemokine receptor known as CCR7.
Synonyms
Small inducible cytokine A21, CCL21, Beta chemokine exodus-2, 6Ckine, Secondary lymphoid-tissue chemokine, SLC, chemokine (C-C motif) ligand 21, ECL, CKb9, TCA4, SCYA21, MGC34555.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Exodus-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL21 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Exodus2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions
Amino Acid Sequence
SDGGGQDCCL KYSQKKIPYS IVRGYRKQEP SLGCPIPAIL FLPRKHSKPE LCANPEEGWV QNLMRRLDQP PAPGKQSPGC RKNRGTSKSG KKGKGSKGCK RTEQTQPSRG.
Background
What is the molecular weight/Mw of CCL21 MOUSE Protein?
CCL21 MOUSE Protein has a total Mw of 12kDa.

What is the source or expression system of CCL21 MOUSE Protein?
Escherichia Coli.

What is the Purity of CCL21 MOUSE Protein?
CCL21 MOUSE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL21 MOUSE Protein?
Determined by its ability to chemoattract total murine T cell population using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

What is the amino acid sequence of CCL21 MOUSE Protein?
SDGGGQDCCL KYSQKKIPYS IVRGYRKQEP SLGCPIPAIL FLPRKHSKPE LCANPEEGWV QNLMRRLDQP PAPGKQSPGC RKNRGTSKSG KKGKGSKGCK RTEQTQPSRG.

What applications can CCL21 MOUSE Protein be used in?
CCL21 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL21 MOUSE Protein?
The endotoxin level is minimal, CCL21 MOUSE Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Super Leptin Antagonist Ovine Recombinant

Product # :

CYT-1245

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Description

Super Leptin Antagonist Ovine Recombinant is a single polypeptide chain containing 146 amino acids, an additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa. Super Ovine Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.

Purity

Greater than 98.0% as determined by:

(a) Gel filtration analysis.

(b) Analysis by SDS-PAGE.

Biological Activity

ProSpec’s super Ovine leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Super Ovine leptin antagonist also inhibits various leptin effects in several in vitro bioassays.

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Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized Super Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of super Ovine leptin antagonist at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization super Ovine leptin antagonist can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Super Leptin Antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 10, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.
Background
Leptin is a hormone which mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviours which save energy. When leptin levels are high, the brain interprets that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Chromosome 11 Open Reading Frame 31 Human Recombinant

Chromosome 11 Open Reading Frame 31, Selenoprotein H, SELH, C17orf10, C11orf31.

Product # :

PRO-1960

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Description

C11ORF31 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (1-122) and having a molecular mass of 15.8 kDa.C11ORF31 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The C11ORF31 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
C11ORF31 (Chromosome 11 Open Reading Frame 31) is a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon which ordinarily signals translation termination. The 3' UTR of selenoprotein genes have a mutual stem-loop structure, the sec insertion sequence (SECIS), which is essential for the recognition of UGA as a Sec codon rather than as a stop signal. The exact function of the C11ORF31 gene is not known, however, selenoproteins are assumed to be responsible for most biomedical effects of dietary selenium. C11ORF31 is involved in a redox-related process.
Synonyms
Chromosome 11 Open Reading Frame 31, Selenoprotein H, SELH, C17orf10, C11orf31.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAPRGRK RKAEAAVVAV AEKREKLANG GEGMEEATVV IEHCTSCRVY GRNAAALSQA LRLEAPELPV KVNPTKPRRG SFEVTLLRPD GSSAELWTGI KKGPPRKLKF PEPQEVVEEL KKYLS.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Complement Component 8, Gamma Human Recombinant

Complement component 8 gamma polypeptide, C8C, complement component C8 gamma chain, MGC142186.

Product # :

PRO-947

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Description

C8G Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 203 amino acids (21-202) and having a molecular mass of 22.6 kDa.The C8G is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The C8G solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.15M NaCl and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
C8, a component of the complement system consists of three polypeptides C8A, C8B and C8G and takes part in the formation of Membrane Attack Complex (MAC). Patients with C8 deficiency are exposed to several bacteria infections. C8G, a member of the lipocalin family and calycin superfamily, is a secreted protein that can bind retinol. C8G is created in the liver, monocytes and fibroblast and has a role in clearing pathogens from an infected host.
Synonyms
Complement component 8 gamma polypeptide, C8C, complement component C8 gamma chain, MGC142186.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQKPQRPRRP ASPISTIQPK ANFDAQQFAG TWLLVAVGSA CRFLQEQGHR AEATTLHVAP QGTAMAVSTF RKLDGICWQV RQLYGDTGVL GRFLLQARGA RGAVHVVVAE TDYQSFAVLY LERAGQLSVK LYARSLPVSD SVLSGFEQRV QEAHLTEDQI FYFPKYGFCE AADQFHVLDE VRR

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fractalkine Human Recombinant (CX3CL1)

Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

Product # :

CHM-235

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Quantity :

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Shipped at Room temp

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Description

Fractalkine Human Recombinant- produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 76 amino acids and having a molecular mass of 8638 Dalton. The Fractalkine is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CX3CL1 was lyophilized from a 0.2μm filtered concentrated (1.0 mg/ml) solution in 20mM Phosphate buffer, pH 7.4, 50mM NaCl.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The Biological activity is calculated by its ability to chemoattract human T-Lymphocytes using a concentration range of 5.0-10.0 ng/ml corresponding to a Specific Activity of 100,000-200,000IU/mg.

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Introduction
Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.
Synonyms
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CX3CL1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CX3CL1 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized CX3CL1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QHHGVTKCNITCSKMTSKIPVALLIHYQQNQASCGKRAIILETRQHRLFCADPKEQW VKDAMQHLDRQAAALTRNG.
Background
What is the molecular weight/Mw of CX3CL1 HUMAN Protein?
CX3CL1 HUMAN Protein has a total Mw of 8.63kDa.

What is the source or expression system of CX3CL1 HUMAN Protein?
Escherichia Coli.

What is the Purity of CX3CL1 HUMAN Protein?
CX3CL1 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CX3CL1 HUMAN Protein?
The Biological activity is calculated by its ability to chemoattract human T-Lymphocytes using a concentration range of 5.0-10.0 ng/ml corresponding to a Specific Activity of 100,000-200,000IU/mg.

What is the amino acid sequence of CX3CL1 HUMAN Protein?
QHHGVTKCNITCSKMTSKIPVALLIHYQQNQASCGKRAIILETRQHRLFCADPKEQW VKDAMQHLDRQAAALTRNG.

What applications can CX3CL1 HUMAN Protein be used in?
CX3CL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CX3CL1 HUMAN Protein?
The endotoxin level is minimal, CX3CL1 HUMAN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

CCAAT/enhancer binding protein C/EBP Gamma Recombinant Human

CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-1.

Product # :

PRO-434

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Description

CEBP-g Recombinant Human His-Tag fusion protein produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 146 (aa 39-147) and having a molecular mass of 16.5 kDa. The DNA binding domain of CEBP-g was purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein contains 20mM Tris-HCl pH7.5, 0.1M NaCl and 5mM b-Mercaptoethanol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
CCAAT/enhancer binding protein(C/EBP) g is a family of transcription factors all contain a highly conserved, basic-leucine zipper domain at the C-terminus that is involved in dimerization and DNA binding. C/EBP family of transcription factors regulates viral and cellular CCAAT/enhancer element-mediated transcription. C/EBP family consist of several related proteins, C/EBP a,b,g,d, that form homodimers and/or form heterodimers with each other. C/EBP proteins contain the bZIP region, which is characterized by two motifs in the C-terminal half of the protein; a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. C/EBP g may cooperate with Fos to bind PRE- enhancer elements.
Synonyms
CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMPGG GGKAVAPSKQ SKKSSPMDRN SDEYRQRRER NNMAVKKSRL KSKQKAQDTL QRVNQLKEEN ERLEAKIKLL TKELSVLKDL FLEHAHNLAD NVQSISTENT TADGDN.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Geminin Human Recombinant

GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.

Product # :

PRO-579

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Description

Geminin Human Recombinant fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 245 amino acids and having a molecular mass of 27.7 kDa.

Source

Escherichia Coli.

Formulation

The protein solution contains 20mM Tris pH 8, 100mM NaCl and 10% glycerol.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
Geminin is a 25 kDa nuclear protein, which inhibits DNA replication and is degraded during the mitotic phase of the cell cycle. Geminin controls replication by binding to the licensing factor Cdt1, and is involved in neural differentiation. In addition, Geminin directly interacts with Six3 and Hox homeodomain proteins during embryogenesis and inhibits their functions. Geminin can also promote DNA replication. Geminin has 2 roles in 2 different stages of the cell cycle: Geminin is a negative regulator of DNA replication during the “S phase” of the cell cycle. Inhibition of Geminin during the “S phase” (by RNAi) results in an additional round of replication of portions of the genome. During the “M phase” of the cell cycle (mitosis) Geminin stabilizes the replication factor Cdt1 promoting DNA replication during the next cell cycle. Moreover, inhibition of Geminin during mitosis (by RNAi) causes destabilization of Cdt1 protein and impairment of DNA replication during the next cell cycle. Geminin thus guarantees that only one round of replication occurs during each cell cycle. It was discovered that Geminin is overexpressed in a number of malignancies and cancer cell lines. This maintains the concept that Geminin has also a positive role in DNA replication and cell cycle progression. Geminin accumulates through S, G2 and M phases of the cell cycle but is absent during the G1 phase. During the metaphase/anaphase transition of mitosis Geminin levels decrease.
Synonyms
GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMNPS MKQKQEEIKE NIKNSSVPRR TLKMIQPSAS GSLVGRENEL SAGLSKRKHR NDHLTSTTSS PGVIVPESSE NKNLGGVTQE SFDLMIKENP SSQYWKEVAE KRRKALYEAL KENEKLHKEI EQKDNEIARL KKENKELAEV AEHVQYMAEL IERLNGEPLD NFESLDNQEF DSEEETVEDS LVEDSEIGTC AEGTVSSSTD
AKPCI.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Charged Multivesicular Body Protein 6 Human Recombinant

Charged multivesicular body protein 6, Chromatin-modifying protein 6, Vacuolar protein sorting-associated protein 20, Vps20, hVps20, CHMP6.

Product # :

PRO-1085

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Description

CHMP6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-201 a.a) and having a molecular mass of 26.1kDa (Molecular size on SDS-PAGE will appear higher).CHMP6 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CHMP6 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Charged multivesicular body protein 6 (CHMP6) is a member of the SNF7 family. The CHMP6 protein is a core component of the endosomal sorting necessary for transport complex III (ESCRT-III) that is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) which are produced by invagination and scission from the limiting membrane of the endosome and generally are transported to lysosomes facilitating degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids.
Synonyms
Charged multivesicular body protein 6, Chromatin-modifying protein 6, Vacuolar protein sorting-associated protein 20, Vps20, hVps20, CHMP6.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMGNLFG RKKQSRVTEQ DKAILQLKQQ RDKLRQYQKR IAQQLERERA LARQLLRDGR KERAKLLLKK KRYQEQLLDR TENQISSLEA MVQSIEFTQI EMKVMEGLQF GNECLNKMHQ VMSIEEVERI LDETQEAVEY QRQIDELLAG SFTQEDEDAI LEELSAITQE QIELPEVPSE PLPEKIPENV PVKARPRQAE LVAAS.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Calcium Binding Protein P22 Human Recombinant

CHP, CHP Human, Calcium-binding protein p22, Calcium-binding protein CHP, Calcineurin homologous protein, Calcineurin B homolog, SLC9A1BP.

Product # :

PRO-847

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Description

CHP Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (1-195 a.a.) and having a molecular mass of 24.7 kDa. The CHP is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CHP Human solution containing 20mM Tris-HCl pH-7.5 & 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Calcium-binding protein P22 is a phosphoprotein that binds to the sodium-hydrogen exchangers (NHEs). CHP is an essential cofactor which maintains the physiological activity of NHE family members. CHP has protein sequence resemblance to calcineurin B and it is also identified to be an endogenous inhibitor of calcineurin activity.CHP is necessary for constitutive membrane traffic. CHP Inhibits GTPase-stimulated Na(+)/H(+) exchange. CHP inhibits calcineurin phosphatase activity. Required for activity of SLC9A1/NHE1.
Synonyms
CHP, CHP Human, Calcium-binding protein p22, Calcium-binding protein CHP, Calcineurin homologous protein, Calcineurin B homolog, SLC9A1BP.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MMGSRASTLL RDEELEEIKK ETGFSHSQIT RLYSRFTSLD KGENGTLSRE DFQRIPELAI NPLGDRIINA FFPEGEDQVN FRGFMRTLAH FRPIEDNEKS KDVNGPEPLN SRSNKLHFAF RLYDLDKDEK ISRDELLQVL RMMVGVNISD EQLGSIADRT IQEADQDGDS AISFTEFVKV LEKVDVEQKM SIRFLH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Creatine Kinase Brain Human Recombinant, His Tag

EC 2.7.3.2, Creatine kinase B chain, Creatine kinase B type, CKB, CKBBB, B-CK, Creatine Kinase Brain.

Product # :

CKI-274

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Description

CKBB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (1-381 a.a.) and having a molecular mass of 44.8 kDa. The CKB is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CKBB Human solution containing 20mM Trsi pH-8, 1mM DTT, & 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
CKB is a cytoplasmic enzyme that takes part in energy homeostasis. CKB enzyme reversibly catalyzes the transfer of phosphate among ATP and various phosphogens such as creatine phosphate. CKB functions as a homodimer in the brain as well as in different tissues, and as a heterodimer with a similar muscle isozyme in heart. Creatine kinases supply the energy of phosphate hydrolysis essential to drive the normal role of many cellular systems including muscle, tumor and cancer cells.
Synonyms
EC 2.7.3.2, Creatine kinase B chain, Creatine kinase B type, CKB, CKBBB, B-CK, Creatine Kinase Brain.
Physical Appearance
Sterile filtered colorless solution.
Stability
CKBB Human although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD
RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

GRO-beta/MIP-2 Rat Recombinant (CXCL2)

Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta, CINC-3.

Product # :

CHM-372

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Description

GRO-Beta Rat Recombinant also called Rat MIP-2 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7923 Dalton. The GRO-b is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 99.0% as determined by SDS-PAGE.

Biological Activity

The biological activity was determined by its ability to chemoattract total human neutrophils using a concentration range of 1.0-10.0 ng/ml, corresponding to a specific activity of 100,000-1,000,000 units/mg.

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Introduction
Chemokine (C-X-C motif) ligand 2 (CXCL2) is a small cytokine belonging to the CXC chemokine family that is also called macrophage inflammatory protein 2-alpha (MIP2-alpha), Growth-regulated protein beta (Gro-beta) and Gro oncogene-2 (Gro-2). CXCL2 is 90% identical in amino acid sequence as a related chemokine, CXCL1. This chemokine is secreted by monocytes and macrophages and is chemotactic for polymorphonuclear leukocytes and hematopoietic stem cells. The gene for CXCL2 is located on human chromosome 4 in a cluster of other CXC chemokines. CXCL2 mobilizes cells by interacting with a cell surface chemokine receptor called CXCR2.
Synonyms
Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta, CINC-3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GRO-b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL2 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized GRO-beta Rat in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VVVASELRCQ CLTTLPRVDF KNIQSLTVTP PGPHCAQTEV IATLKDGHEV CLNPEAPLVQ RIVQKILNKG KAN.
Background
What is the molecular weight/Mw of CXCL2 RAT Protein?
CXCL2 RAT Protein has a total Mw of 7.92kDa.

What is the source or expression system of CXCL2 RAT Protein?
Escherichia Coli.

What is the Purity of CXCL2 RAT Protein?
CXCL2 RAT Protein is >99% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL2 RAT Protein?
The biological activity was determined by its ability to chemoattract total human neutrophils using a concentration range of 1.0-10.0 ng/ml, corresponding to a specific activity of 100,000-1,000,000 units/mg.

What is the amino acid sequence of CXCL2 RAT Protein?
VVVASELRCQ CLTTLPRVDF KNIQSLTVTP PGPHCAQTEV IATLKDGHEV CLNPEAPLVQ RIVQKILNKG KAN.

What applications can CXCL2 RAT Protein be used in?
CXCL2 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL2 RAT Protein?
The endotoxin level is minimal, CXCL2 RAT Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

GRO-Gamma Rat Recombinant (CXCL3), CINC-2 alpha

Cytokine-induced neutrophil chemoattractant 2, CINC2, CINC-2, Macrophage inflammatory protein 2-alpha.

Product # :

CHM-258

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Description

GRO-g Rat Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7.8kDa. The CXCL3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Rat CXCL3 lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Determined by its ability to chemoattract 293 transfected CXCR2 cells using a concentration range of 10-100 ng/ml, corresponding to a specific activity of 10,000-100,000 units/mg.

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Introduction
Chemokine (C-X-C motif) ligand 3 (CXCL3) is a small cytokine belonging to the CXC chemokine family that is also known as GRO3 oncogene (GRO3), GRO protein gamma (GROg) and macrophage inflammatory protein-2-beta (MIP2b). CXCL3 controls migration and adhesion of monocytes and mediates it effects on its target cell by interacting with a cell surface chemokine receptor called CXCR2. The gene for CXCL3 is located on chromosome 4 in a cluster of other CXC chemokines.
Synonyms
Cytokine-induced neutrophil chemoattractant 2, CINC2, CINC-2, Macrophage inflammatory protein 2-alpha.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GRO-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized GRO-gamma in sterile 18Mcm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
RELRCQCLKT LPRVDFENIQ SLTVTPPGPH CTQTEVIATL KDGQEVCLNP QAPRLQKIIQ KLLKSDKSS.
Background
What is the molecular weight/Mw of CXCL3 RAT ALPHA Protein?
CXCL3 RAT ALPHA Protein has a total Mw of 7.8kDa.

What is the source or expression system of CXCL3 RAT ALPHA Protein?
Escherichia Coli.

What is the Purity of CXCL3 RAT ALPHA Protein?
CXCL3 RAT ALPHA Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL3 RAT ALPHA Protein?
Determined by its ability to chemoattract 293 transfected CXCR2 cells using a concentration range of 10-100 ng/ml, corresponding to a specific activity of 10,000-100,000 units/mg.

What is the amino acid sequence of CXCL3 RAT ALPHA Protein?
RELRCQCLKT LPRVDFENIQ SLTVTPPGPH CTQTEVIATL KDGQEVCLNP QAPRLQKIIQ KLLKSDKSS.

What applications can CXCL3 RAT ALPHA Protein be used in?
CXCL3 RAT ALPHA Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL3 RAT ALPHA Protein?
The endotoxin level is minimal, CXCL3 RAT ALPHA Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Macrophage-Derived Chemokine (CCL22) Rat Recombinant

C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1, CC chemokine ABCD-1, Activated B and dendritic cell-derived, DCBCK.

Product # :

CHM-279

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Description

CCL22 Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 68 amino acids and having a molecular mass of 7.9kDa. The Rat CCL22 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH7.4.

Purity

Greater than 97.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Determined by its ability to chemoattract human activated lymphocytes using a concentration range of 10.0-100.0 ng/ml.

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Introduction
MDC (CCL22) is a small cytokine that belongs to the CC chemokine family. CCL22 is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16.
MDC shows chemotactic activity for natural killer cells, chronically activated T lymphocytes, monocytes and dendritic cells. On the other hand, MDC shows a mild activity for primary activated T lymphocytes and has no chemoattractant activity for neutrophils, eosinophils and resting T lymphocytes. MDC may also have a role in the trafficking of activated T lymphocytes to inflammatory sites and other aspects of activated T lymphocyte physiology. MDC interacts with cell surface chemokine receptors CCR4.
CCL22 is vastly expressed in macrophage and in monocyte-derived dendritic cells, and thymus. CCL22 is also found in the lymph node, appendix, activated monocytes, resting and activated macrophages. Lower expression of CCL22 can be seen in the lung and the spleen and very weak expression in the small intestine. In the lymph node CCL22 is expressed in a mature subset of Langerhans' cells (CD1a+ and CD83+).
Furthermore, CCL22 is expressed in atopic dermatitis, allergic contact dermatitis skin, and psoriasis, in both the epidermis and dermis. In addition, MDC has a role in hindering progression of lung cancer. Moreover, significantly higher CCL22 expression is linked to gastric cancer.
Synonyms
C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1, CC chemokine ABCD-1, Activated B and dendritic cell-derived, DCBCK.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MDC although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution MDC should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized MDC in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GPYGANVEDS ICCQDYIRHP LPPRFVKEFY WTSKSCRKPG VVLITIKNRD ICADPRMLWV KKILHKLA.
Background
What is the molecular weight/Mw of CCL22 RAT Protein?
CCL22 RAT Protein has a total Mw of 7.9kDa.

What is the source or expression system of CCL22 RAT Protein?
Escherichia Coli.

What is the Purity of CCL22 RAT Protein?
CCL22 RAT Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL22 RAT Protein?
Determined by its ability to chemoattract human activated lymphocytes using a concentration range of 10.0-100.0 ng/ml.

What is the amino acid sequence of CCL22 RAT Protein?
GPYGANVEDS ICCQDYIRHP LPPRFVKEFY WTSKSCRKPG VVLITIKNRD ICADPRMLWV KKILHKLA

What applications can CCL22 RAT Protein be used in?
CCL22 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL22 RAT Protein?
The endotoxin level is minimal, CCL22 RAT Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Relaxin-3 Human Recombinant

Relaxin 3, Prorelaxin H3, RXN3, Insl7, ZINS4, H3, Relaxin 3 (H3), Relaxin-3, RLN3.

Product # :

PRO-2176

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Description

Relaxin-3 Human Recombinant produced in E.Coli is a disulfide-linked heterodimeric, non-glycosylated, polypeptide chain containing 24 amino acids for A chain and 27 amino acids for B chain and having a molecular mass of 2.5kDa for A chain and 3kDa for B chain.The Relaxin-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as measured by cAMP accumulation in human THP-1 cells, is less than 17.5ng/ml.

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Introduction
Relaxin-3 (RLN3) belongs to the relaxin family. Relaxins are endocrine and autocrine/paracrine hormones. Relaxin, which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. Unlike human Relaxins 1 and 2, Relaxin 3 does not seem to have a role in reproduction; however it is involved in stress response in the brain stem. RLN3 is the only known ligand for the G-protein-coupled receptor GPCR135, titled RXFP3. In addition, RLN3 binds the LGR7 (RXFP1) receptor, however with lower affinity than Relaxin-2. Even though binding of RLN3 to LGR7 increases intracellular cAMP, binding to GPCR135 suppresses cAMP accumulation, indicating coupling to Gi, Go, or Gz by this receptor.
Synonyms
Relaxin 3, Prorelaxin H3, RXN3, Insl7, ZINS4, H3, Relaxin 3 (H3), Relaxin-3, RLN3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized RLN3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Relaxin-3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized RLN3 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
A chain: DVLAGLSSSC CKWGCSKSEI SSLC.
B chain: RAAPYGVRLCG REFIRAVIFT CGGSRW.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Granulocyte Macrophage-Colony Stimulating Factor Porcine Recombinant

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

Product # :

CYT-1095

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Shipped at Room temp

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Description

Granulocyte Macrophage-Colony Stimulating Factor Porcine Recombinant produced in E. coli is a non-glycosylated monomer chain containing 128 amino acids and having a molecular mass of 14.5kDa. GMCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a sterile (0.2µm) filtered solution containing 10mM sodium phosphate, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as determined by TF-1 cell proliferation is 4.52ng/ml corresponding to a specific activity which is 2.2 x 10^5 units/mg.

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Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of GMCSF is found extracellularly as a homodimer. GMCSF has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GMCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized GMCSF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK.
Background
What is the molecular weight/Mw of GM-CSF PORCINE Protein?
GM-CSF PORCINE Protein has a total Mw of 14.5kDa.

What is the source or expression system of GM-CSF PORCINE Protein?
Escherichia Coli.

What is the Purity of GM-CSF PORCINE Protein?
GM-CSF PORCINE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GM-CSF PORCINE Protein?
The ED50, as determined by TF-1 cell proliferation is 4.52ng/ml corresponding to a specific activity which is 2.2 x 10^5 units/mg.

What is the amino acid sequence of GM-CSF PORCINE Protein?
MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK.

What applications can GM-CSF PORCINE Protein be used in?
GM-CSF PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GM-CSF PORCINE Protein?
The endotoxin level is minimal, GM-CSF PORCINE Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Cytokeratin 8, Mouse Anti Human

Keratin type II cytoskeletal 8, Cytokeratin-8, CK-8, Keratin-8, K8, KRT8, CYK8, KO, CK8, K2C8, CARD2.

Product # :

ANT-470

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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formulation
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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
Cytokeratin 8 (KRT8) belongs to the type II keratin family clustered on the long arm of chromosome 12. Type I and type II keratins heteropolymerize to form intermediate-sized filaments in the cytoplasm of epithelial cells. KRT8 typically dimerizes with keratin 18 to form an intermediate filament in simple single-layered epithelial cells. KRT8 has a role in retaining cellular structural integrity and also functions in signal transduction and cellular differentiation. KRT8 gene mutations cause cryptogenic cirrhosis.
Synonyms
Keratin type II cytoskeletal 8, Cytokeratin-8, CK-8, Keratin-8, K8, KRT8, CYK8, KO, CK8, K2C8, CARD2.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human KRT8 mAb, clone PAT3D11A, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human KRT8 protein purified from E. coli.
Ig Subclass
Mouse IgG3 heavy chain and Kappa light chain.
Clone
PAT3D11A.
Applications
The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Thyroid Stimulating Hormone Canine Recombinant

Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follitropin alpha chain, Follicle-stimulating hormone alpha chain, FSH-alpha, Lutropin alpha chain, Luteinizing hormone alpha chain, LSH-alpha, Thyrotropin alpha chain, Thyroid-stimulating hormone alpha chain, TSH-alpha, Choriogonadotropin alpha chain, Chorionic gonadotrophin alpha subunit, CG-alpha, Thyrotropin subunit beta, Thyroid-stimulating hormone subunit beta, TSH-beta, TSH-B, Thyrotropin beta chain, Thyrotropin alfa.

Product # :

HOR-049

Price :

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Shipping Method :

Shipped at Room temp

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Description

TSH Canine is a heterodimeric glycoprotein consisting of 2 non-covalently linked subunits, an alpha subunit (96 a.a) and a beta subunit (118 a.a). TSH Canine is produced by co-expression of the alpha and beta subunits of TSH. Beta subunit contains alanine instead of valine at position 81.

Source

Mammalian cell line.

Formulation

TSH was lyophilized from 150mM NaCl, 10mM K-phosphate, pH 7.4, 0.1% CHAPS and 100mM D-mannitol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Synonyms
Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follitropin alpha chain, Follicle-stimulating hormone alpha chain, FSH-alpha, Lutropin alpha chain, Luteinizing hormone alpha chain, LSH-alpha, Thyrotropin alpha chain, Thyroid-stimulating hormone alpha chain, TSH-alpha, Choriogonadotropin alpha chain, Chorionic gonadotrophin alpha subunit, CG-alpha, Thyrotropin subunit beta, Thyroid-stimulating hormone subunit beta, TSH-beta, TSH-B, Thyrotropin beta chain, Thyrotropin alfa.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TSH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thyroid Stimulating Hormone should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized TSH in deionized H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Thyroid Stimulating Hormone (TSH), a pivotal glycoprotein hormone secreted by the anterior pituitary gland, stands as the master regulator of thyroid function. Its intricate control over thyroid hormone synthesis and secretion makes it a linchpin in the delicate balance of the endocrine system. The study of TSH, particularly in the form of TSH Recombinant Protein, has not only provided profound insights into thyroid physiology but has also revolutionized diagnostic methods, therapeutic interventions, and our understanding of various thyroid disorders. This research delves into the multifaceted realm of TSH, exploring its structural intricacies, physiological roles, and its far-reaching implications in both clinical and research settings.
Structural Insights into TSH:
TSH, a heterodimeric protein consisting of alpha and beta subunits, possesses a distinctive structure crucial for its biological activity. The beta subunit contains a unique hinge region, allowing flexibility in its interactions with the thyroid follicular cells. Understanding these structural nuances is fundamental for comprehending TSH's receptor binding, signaling cascades, and its intricate feedback mechanisms governing thyroid hormone production.
Physiological Significance in Thyroid Regulation:
TSH orchestrates thyroid function by binding to its specific receptors on the thyroid gland, stimulating iodine uptake, thyroid hormone synthesis, and secretion. This process is indispensable for maintaining the body's metabolism, energy balance, and overall growth and development. TSH's meticulous control over thyroid activity ensures the precise release of thyroid hormones, essential for numerous physiological processes and maintaining homeostasis.
Diagnostic and Therapeutic Applications:
In the realm of diagnostics, TSH assays utilizing TSH Recombinant Protein have revolutionized the detection and monitoring of thyroid disorders, particularly hypothyroidism and hyperthyroidism. By measuring TSH levels, clinicians can assess thyroid function, enabling early diagnosis and personalized treatment strategies. Moreover, recombinant TSH finds applications in diagnostic imaging, enhancing the accuracy of radioiodine scans for thyroid cancer diagnosis and treatment.
Innovative Therapies and Future Prospects:
Recombinant TSH has paved the way for innovative therapeutic interventions, particularly in the management of thyroid cancer. Thyroid remnant ablation, a crucial step in thyroid cancer treatment, involves the administration of radioiodine following recombinant TSH stimulation, maximizing the therapeutic efficacy while minimizing the radiation exposure to surrounding tissues. Ongoing research explores the potential of TSH receptor agonists and antagonists, offering new avenues for targeted therapies in thyroid-related disorders.
TSH Recombinant Protein, with its profound influence on thyroid function and its applications in diagnostics and therapeutics, stands at the forefront of endocrine research. Its intricate roles in thyroid regulation, metabolism, and growth highlight its significance in human physiology. As our understanding of TSH deepens, it not only aids in the development of innovative treatments but also opens new avenues for exploring the complex interplay between hormones, receptors, and physiological responses. This research not only illuminates the vital role of TSH but also underscores its potential in shaping the future of thyroid-related healthcare.
What is the source or expression system of TSH CANINE Protein?
Mammalian cell line.

What is the Purity of TSH CANINE Protein?
TSH CANINE Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of TSH CANINE Protein?
The biological functionality of TSH CANINE Protein will be determined in the future.

What applications can TSH CANINE Protein be used in?
TSH CANINE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for TSH CANINE Protein?
The endotoxin level is minimal, TSH CANINE Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

AOD-9604

Product # :

HOR-064

Price :

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Description

AOD-9604 is a synthetic single, non-glycosylated polypeptide chain containing 16 amino acids, having a molecular mass of 1815 Dalton and a Molecular formula of C78H123N23O23 S2.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by RP-HPLC.

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized AOD-9604 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution AOD-9604 should be stored at 4°C between 2-7 days and for future use below -18°C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized AOD-9604 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-Tyr-Leu-Arg-Ile-Val-Gln-Cys-Arg-SerVal-Glu-Gly-Ser-Cys-Gly-Phe-OH (Disulfide bond).
Background
AOD-9604 is a synthetic analog of the C-terminal fragment (177–191) AOD-9604 stimulates lipolysis (fat breakdown) without the unwanted growth-promoting or insulin-antagonizing effects of full-length hGH. AOD-9604 is a potent lipolytic tool in animal models and researchers focus on its regenerative properties in joint health and its ability to modulate beta3 adrenergic receptors without the systemic risks of growth hormone.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Carbonyl Reductase-1 PAT2D6AT, Mouse Anti Human

CBR, hCBR1, SDR21C1, CBR1, Carbonyl reductase [NADPH] 1, NADPH-dependent carbonyl reductase 1, Prostaglandin-E(2) 9-reductase, Prostaglandin 9-ketoreductase, 15-hydroxyprostaglandin dehydrogenase [NADP+], CRN.

Product # :

ANT-584

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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formulation
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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
CBR1 is one of numerous monomeric, NADPH-dependent oxidoreductases having ubiquistly specificity for carbonyl compounds. CBR1 is broadly distributed in human tissues. CBR1 metabolizes toxic environmental quinones and pharmacological relevant substrates such as the anticancer doxorubicin. CBR1 converts prostaglandin E2 to prostaglandin F2-alpha.
Synonyms
CBR, hCBR1, SDR21C1, CBR1, Carbonyl reductase [NADPH] 1, NADPH-dependent carbonyl reductase 1, Prostaglandin-E(2) 9-reductase, Prostaglandin 9-ketoreductase, 15-hydroxyprostaglandin dehydrogenase [NADP+], CRN.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human CBR1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CBR1 amino acids 1-277 purified from E. coli.
Ig Subclass
Mouse IgG2a heavy chain and k light chain.
Clone
PAT2D6AT.
Applications
CBR1 antibody has been tested by ELISA, Western blot analysis, ICC/IF and Flow cytometry to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
CBR1 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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