Search: 1000 results found for "Chromogranin"

Description:

Somatostatin

Growth hormone release-inhibiting factor, SST, SMS, SMST, GHIH.

Product # :

HOR-299

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Description

Somatostatin Synthetic is a single, non-glycosylated polypeptide chain containing 14 amino acids, having a molecular mass of 1637.9 Dalton and a Molecular formula of C76H104N18O19S2. The CAS# is 38916-34-6.

Formulation

The protein was lyophilized with no additives.

Purity

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

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Introduction
Somatostatin (also known as growth hormone inhibiting hormone (GHIH) or somatotropin release-inhibiting hormone (SRIF) is a peptide hormone that regulates the endocrine systemand affects neurotransmission and cell proliferation via interaction with G-protein-coupled somatostatin receptors and inhibition of the release of numerous secondary hormones. Somatostatin has two active forms produced by alternative cleavage of a single preproprotein: one of 14 amino acids, the other of 28 amino acids.
Synonyms
Growth hormone release-inhibiting factor, SST, SMS, SMST, GHIH.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SST although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Somatostatin 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 Somatostatin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Ala-Gly-Cys-Lys-Asn-Phe- Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys-OH.
Background
What is the molecular weight/Mw of SOMATOSTATIN Protein?
SOMATOSTATIN Protein has a total Mw of 1.637kDa.

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

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

What is the amino acid sequence of SOMATOSTATIN Protein?
Ala-Gly-Cys-Lys-Asn-Phe- Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys-OH.

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

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

Who supplies SOMATOSTATIN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of SOMATOSTATIN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

Corticotropin Releasing Hormone (13-87 a.a.) Human Recombinant

CRF, Corticotropin-Releasing Factor.

Product # :

HOR-054

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Description

The CRH Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The CRH His-Tagged Fusion Protein, produced in E. coli, is a 15kDa protein containing 75 amino acid residues of the CRH Human, 13-87 amino acids.

Source

Escherichia Coli.

Formulation

Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Synonyms
CRF, Corticotropin-Releasing Factor.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized CRH 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 deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Background
CRH is a neuropeptide which regulates body's response to stress. CRH stimulates the release of ACTH from the pituitary gland which triggers the adrenal glands to produce cortisol. CRH takes part in the hypothalamic-pituitary-adrenal axis which controls the production of cortisol and other glucocorticoids. CRH is synthesized in different tissues such as the brainstem, hypothalamus and peripheral organs. In Pregnancy, CRH regulates parturition and fetal development.

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:

Gastric Inhibitory Polypeptide Human Recombinant

Gastric inhibitory polypeptide, GIP, Incretin hormone.

Product # :

PRO-1438

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Description

GIP Human Recombinant produced in E. coli is a single polypeptide chain containing 155 amino acids (22-153) and having a molecular mass of 17.3kDa. GIP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The GIP solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 50% glycerol 0.1M NaCl and 2mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Gastric Inhibitory Polypeptide (GIP) which is a significant hormone of the enteroinsular axis has a functional profile of possible therapeutic value for type 2 diabetes. GIP is an important incretin hormone released into the circulation from endocrine K-cells of the duodenum and jejunum after ingestion of food1. GIP was evaluated for his ability to elevate cellular cAMP production. GIP promotes plasma triglyceride clearance in response to oral fat loading.
Synonyms
Gastric inhibitory polypeptide, GIP, Incretin hormone.
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 MGSEKKEGHF SALPSLPVGS HAKVSSPQPR GPRYAEGTFI SDYSIAMDKI HQQDFVNWLL AQKGKKNDWK HNITQREARA LELAGQANRK EEEAVEPQSS PAKNPSDEDL LRDLLIQELL ACLLDQTNLC RLRSR.

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:

Secernin 1 Human Recombinant

Secernin-1, SES1, KIAA0193, Secernin 1.

Product # :

PRO-2212

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Description

SCRN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 437 amino acids (1-414 a.a) and having a molecular mass of 48.8kDa. SCRN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SCRN1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) , 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Secernin 1 (SCRN1) which is a member of the peptidase C69 family, regulates exocytosis in mast cells. SCRN1 increases both the level of secretion and the sensitivity of mast cells to stimulation with calcium.
Synonyms
Secernin-1, SES1, KIAA0193, Secernin 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
GSSHHHHHH SSGLVPRGSH MGSMAAAPPS YCFVAFPPRA KDGLVVFGKN SARPRDEVQE VVYFSAADHE PESKVECTYI SIDQVPRTYA IMISRPAWLW GAEMGANEHG VCIANEAINT REPAAEIEAL LGMDLVRLGL ERGETAKEAL DVIVSLLEEH GQGGNYFEDA NSCHSFQSAY LIVDRDEAWV LETIGKYWAA EKVTEGVRCI CSQLSLTTKM DAEHPELRSY AQSQGWWTGE GEFNFSEVFS PVEDHLDCGA GKDSLEKQEE SITVQTMMNT LRDKASGVCI DSEFFLTTAS GVSVLPQNRS SPCIHYFTGT PDPSRSIFKP FIFVDDVKLV PKTQSPCFGD DDPAKKEPRF QEKPDRRHEL YKAHEWARAI IESDQEQGRK LRSTMLELEK QGLEAMEEIL TSSEPLDPAE VGDLFYDCVD TEIKFFK.

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:

Oxyntomodulin Porcine Recombinant

Product # :

HOR-292

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Description

Oxyntomodulin Porcine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 37 amino acids and having a molecular mass of 4420.86 Dalton. The OXM is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

Purity

Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
OXM a 37 amino acid peptide which contains the glucagon sequence extended by a C-terminal basic octapeptide, its primary structure is identical in all mammals except in pig and cattle. OXM is released from the gut during digestion, together with glicentin another octapeptide containing molecule. It is considered as a putative physiological regulator of gastric acid secretion, it inhibits histamine.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Oxyntomodulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OXM 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 Oxyntomodulin in 20mM acetic acid.
Amino Acid Sequence
His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-Gln-Asp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr-Lys-Arg-Asn-Lys-Asn-Asn-Ile-Ala.
Background
What is the molecular weight/Mw of OXYNTOMODULIN Protein?
OXYNTOMODULIN Protein has a total Mw of 4.420kDa.

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

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

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

What is the amino acid sequence of OXYNTOMODULIN Protein?
His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-Gln-Asp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr-Lys-Arg-Asn-Lys-Asn-Asn-Ile-Ala.

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

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

Who supplies recombinant OXYNTOMODULIN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of OXYNTOMODULIN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

Regenerating Islet-Derived 1 Alpha Human Recombinant

Lithostathine-1-alpha, Pancreatic stone protein, PSP, Pancreatic thread protein, PTP, Islet of Langerhans regenerating protein, REG, Regenerating protein I alpha, Islet cells regeneration factor, ICRF, REG1A, PSPS, P19, PSPS1, MGC12447.

Product # :

PRO-289

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Description

The Recombinant Human REG 1 alpha is produced with N-terminal fusion His Tag. The Recombinant Human REG 1 alpha His-Tagged Fusion Protein, has a molecular weight of 17.8 kDa protein containing 144 amino acid residues of the Human REG 1 alpha and 12 additional amino acid residues – His Tag.

Source

Escherichia Coli.

Formulation

Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 5mM Tris, 25mM NaCl, pH 7.5.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
REG protein was shown to be stimulated during the regeneration of pancreatic islets. Since then, many Reg-related proteins have been identified in humans and other animals. In human, the four REG family genes, i.e., REG 1 alpha, REG 1 beta, REG-related sequence (RS) and HIP/PAP, have so far been isolated. These Reg-related proteins are classified into four subfamilies according to their amino-acid sequences, but they share a similar structure and physiological function. Reg protein is a growth factor for pancreatic beta cells and also suggests that the administration of Reg protein could be used as another therapeutic approach for diabetes mellitus. Human REG cDNA which encodes a 166-amino acid protein with a 22-amino acid signal peptide. The amino acid sequence of human REG protein has 68% homology to that of rat Reg protein.
Reg I was found to be expressed mainly in pancreatic beta and acinoductular cells as well as gastric fundic enterochromaffin-like (ECL) cells. Reg I production in ECL cells is stimulated by gastrin, as well as by the proinflammatory cytokine, cytokine-induced neutrophil chemoattractant (CINC)-2Beta. In patients with chronic hypergastrinemia, Reg production is stimulated, with the increased proliferation of gastric mucosal cells. Patients with Helicobacter pylori infection also showed increased Reg production in the gastric mucosa, partly via increased plasma gastrin concentration and partly via increased proinflammatory cytokine production. The serum concentration of the reg-protein was significantly higher in patients with various pancreatic diseases than in normal controls, and was also significantly higher in patients with acute pancreatitis or chronic relapsing pancreatitis than in patients with chronic pancreatitis. Furthermore, the serum PSP/reg-protein concentration was also significantly increased in liver cirrhosis, choledocholithiasis, and various cancers of the digestive system.
Synonyms
Lithostathine-1-alpha, Pancreatic stone protein, PSP, Pancreatic thread protein, PTP, Islet of Langerhans regenerating protein, REG, Regenerating protein I alpha, Islet cells regeneration factor, ICRF, REG1A, PSPS, P19, PSPS1, MGC12447.
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
Add deionized water to a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHAS HMQEAQTELP QARISCPEGT NAYRSYCYYF NEDRETWVDA DLYCQNMNSG NLVSVLTQAE GAFVASLIKE SGTDDFNVWI GLHDPKKNRR WHWSSGSLVS YKSWGIGAPS SVNPGYCVSL TSSTGFQKWK DVPCEDKFSF VCKFKN.

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:

Thymosin β4

Thymosin beta-4. TB500, TB-500

Product # :

HOR-275

Price :

Quantity :

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Description

Thymosin b4 is a 43 amino acid peptide which is regarded as the main intracellular G-actin sequestering peptide. It has a molecular weight of 4963.55 Da, and its molecular formula is: C212H350N56O78S1. Extracellular Thymosin b4 may contribute to physiological processes such as angiogenesis, wound healing, and regulation of inflammation.

Formulation

The protein (1mg/ml) was lyophilized with no additives.

Purity

Greater than 98.0% as determined by RP-HPLC.

More Info

Introduction
Thymosin is a hormone secreted from the thymus. Its primary function is to stimulate the production of T cells, which are an important part of the immune system. Thymosin also assists in the development of B cells to plasma cells to produce antibodies. The predominant form of thymosin, thymosin b4, is a member of a highly conserved family of actin monomer-sequestering proteins. b-thymosins are the primary regulators of unpolymerized actin, and are essential for maintaining the small cytoplasmic pool of free G-actin monomers required for rapid filament elongation and allowing for the flux of monomers between the thymosin-bound pool and F-actin.
Synonyms
Thymosin beta-4. TB500, TB-500
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Thymosin b4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution T beta 4 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 Thymosin beta-4 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Thymosin b4 has an a.a. sequence of Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser-OH.
Background
What is the molecular weight/Mw of THYMOSIN BETA 4 Protein?
THYMOSIN BETA 4 Protein has a total Mw of 4.96kDa.

What is the Purity of THYMOSIN BETA 4 Protein?
THYMOSIN BETA 4 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of THYMOSIN BETA 4 Protein?
The biological functionality of THYMOSIN BETA 4 Protein will be determined in the future.

What is the amino acid sequence of THYMOSIN BETA 4 Protein?
Thymosin b4 has an a.a. sequence of Ac-Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser-OH.
What applications can THYMOSIN BETA 4 Protein be used in?
THYMOSIN BETA 4 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for THYMOSIN BETA 4 Protein?
The endotoxin level is minimal, THYMOSIN BETA 4 Protein was purified using conventional chromatography techniques.

Who supplies THYMOSIN BETA 4 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of THYMOSIN BETA 4?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

Decorin Human Recombinant, Sf9

Decorin, Decorin Proteoglycan, Bone Proteoglycan II, SLRR1B, PG-S2, CSCD, PG40, Dermatan Sulphate Proteoglycans II, Small Leucine-Rich Protein 1B, Proteoglycan Core Protein, DSPG2, PGII, PGS2, Decorin, Bone proteoglycan II, PG-S2, , PG40.

Product # :

PRO-2232

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Quantity :

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Description

DCN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 335 amino acids (31-359a.a.) and having a molecular mass of 37.1kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). DCN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

DCN protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.
Synonyms
Decorin, Decorin Proteoglycan, Bone Proteoglycan II, SLRR1B, PG-S2, CSCD, PG40, Dermatan Sulphate Proteoglycans II, Small Leucine-Rich Protein 1B, Proteoglycan Core Protein, DSPG2, PGII, PGS2, Decorin, Bone proteoglycan II, PG-S2, , PG40.
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
DEASGIGPEV PDDRDFEPSL GPVCPFRCQC HLRVVQCSDL GLDKVPKDLP PDTTLLDLQN NKITEIKDGD FKNLKNLHAL ILVNNKISKV SPGAFTPLVK LERLYLSKNQ LKELPEKMPK TLQELRAHEN EITKVRKVTF NGLNQMIVIE LGTNPLKSSG IENGAFQGMK KLSYIRIADT NITSIPQGLP PSLTELHLDG NKISRVDAAS LKGLNNLAKL GLSFNSISAV DNGSLANTPH LRELHLDNNK LTRVPGGLAE HKYIQVVYLH NNNISVVGSS DFCPPGHNTK KASYSGVSLF SNPVQYWEIQ PSTFRCVYVR SAIQLGNYKH HHHHH.

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:

Thymopentin

Product # :

HOR-241

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Thymopentin has a molecular formula of C30H49N9O9, Arg-Lys-Asp-Val-Tyr-OH having an Mw of 679.8 Dalton.

Formulation

The protein (1mg/ml) was lyophilized with no additives.

Purity

Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

What is the molecular weight/Mw of THYMOPENTIN Protein? THYMOPENTIN Protein has a total Mw of 0.67kDa. What is the Purity of THYMOPENTIN Protein? THYMOPENTIN Protein is >99% pure as determined by SDS-PAGE. What is the Biological Activity of THYMOPENTIN Protein? The biological functionality of THYMOPENTIN Protein will be determined in the future. What applications can THYMOPENTIN Protein be used in? THYMOPENTIN Protein can probably be used in western blot, ELISA and Lateral Flow. What is the endotoxin level for THYMOPENTIN Protein? The endotoxin level is minimal, THYMOPENTIN Protein was purified using conventional chromatography techniques.

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Introduction
Thymopentin, also known as TP-5, is a synthetic pentapeptide which is the active site of the naturally occurring hormone thymopoietin with immunomodulating properties (corresponding to the amino acids 32-36 of thymopoietin). Thymopentin enhances the production of thymic T cells and may help restore immunocompetence in immunosuppressed subjects. This agent also augments the effects of ionizing radiation by arresting cancer cells in the G2/M phase of the cell cycle.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Thymopentin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TP-5 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 Thymopentin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

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:

Aprotinin

Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.

Product # :

PRO-285

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Quantity :

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Description

Aprotinin is a natural proteinase inhibitor polypeptide consisting of fifty-eight amino acids {C284H432N84O79S7} arranged in a single polypeptide chain, cross-linked by three disulfide bridges and having a molecular mass of 6512.

Source

Bovine Lung.

Formulation

The protein (1mg/ml) was lyophilized with no additives.

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Introduction
Aprotinin inhibits the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin and trypsin. Aprotinin is present in blood and in most tissues, with a high concentration in lung. Aprotinin inhibits pro-inflammatory cytokine release and maintains glycoprotein homeostasis. In platelets, aprotinin reduces glycoprotein loss (e.g., GpIb, GpIIb/IIIa), while in granulocytes it prevents the expression of pro-inflammatory adhesive glycoproteins (e.g., CD11b).
Synonyms
Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Aprotinin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Aprotinin 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 Aprotinin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Specific Activity
5,940 KIU (Kallikrein Inactivator Units) per mg, 3.3 pH.Eur.U/mg.

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:

Terlipressin

Product # :

HOR-287

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Terlipressin contains 12 amino acids Gly-Gly-Gly-c[Cys-Tyr-Phe-Gln-Asn-Cys]-Pro-Lys-Gly-NH2 and having a molecular weight of 1227.37 Dalton.

Formulation

The protein (1 mg/ml) was lyophilized with no additives.

Purity

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

More Info

Introduction
Terlipressin is similar to a naturally occurring hormone present in the body, known as antidiuretic hormone (ADH) or vasopressin. ADH has two main effects in the body. Firstly, it causes narrowing of blood vessels (vasoconstriction), thereby limiting blood flow to a particular area of the body. It also acts on receptors in the kidney to retain water in the body, which helps to prevent excessive loss of water in the urine. Terlipressin is commonly used to stop bleeding of varices in the food pipe (oesophagus). Varices are fragile distended veins that can occur in various parts of the body such as the oesophagus. This is caused by an increase in blood pressure in certain diseases such as severe liver disease. These fragile varices can rupture and lead to life threatening bleeding. Terlipressin is therefore given to narrow blood vessels, and so restricting blood flow to the varices and stopping the bleeding.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Terlipressin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Terlipressin 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 Terlipressin18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Gly-Gly-Gly-C[Cys-Tyr-Phe-Gln-Asn-Cys]-Pro-Lys-Gly-NH2
Background
What is the molecular weight/Mw of TERLIPRESSIN Protein?
TERLIPRESSIN Protein has a total Mw of 1.227kDa.

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

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

What is the amino acid sequence of TERLIPRESSIN Protein?
Gly-Gly-Gly-c[Cys-Tyr-Phe-Gln-Asn-Cys]-Pro-Lys-Gly-NH2

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

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

Who supplies TERLIPRESSIN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of TERLIPRESSIN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

Decorin Human Recombinant

Decorin, Bone proteoglycan II, PG-S2, PG40, DCN, SLRR1B, CSCD, PGII, PGS2, DSPG2.

Product # :

PRO-1583

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
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Description

DCN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (31-359 a.a) and having a molecular mass of 38.6kDa.DCN is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

DCN protein solution (0.25mg/ml) containing 20mM Tris pH 8.0 and 10% glycerol.

Purity

Greater than 80% as determined by SDS-PAGE.

More Info

Introduction
Decorin (DCN) is a small cellular or pericellular matrix proteoglycan which is closely related in structure to biglycan protein. Decorin is a secreted protein which binds to collagen and fibronectin in extracellular matrix. Decorin appears in different glycoforms, substituted with chondroitin sulfate or dermatan sulfate consistent with the original tissue. DCN contains one attached glycosaminoglycan chain. Decorin influences the rate of fibril formation. Decorin is capable of suppressing the growth of various tumor cell lines. DCN gene defects cause corneal dystrophy. The DCN gene is a candidate gene for Marfan syndrome.
Synonyms
Decorin, Bone proteoglycan II, PG-S2, PG40, DCN, SLRR1B, CSCD, PGII, PGS2, DSPG2.
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 MDEASGIGPE VPDDRDFEPS LGPVCPFRCQ CHLRVVQCSDLGLDKVPKDL PPDTTLLDLQ NNKITEIKDG DFKNLKNLHA LILVNNKISK VSPGAFTPLVKLERLYLSKN QLKELPEKMP KTLQELRAHE NEITKVRKVT FNGLNQMIVI ELGTNPLKSS GIENGAFQGM KKLSYIRIAD TNITSIPQGL PPSLTELHLD GNKISRVDAA SLKGLNNLAKLGLSFNSISA VDNGSLANTP HLRELHLDNN KLTRVPGGLA EHKYIQVVYL HNNNISVVGSSDFCPPGHNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYV RSAIQLGNYK.

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:

Thymulin

Product # :

HOR-047

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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purity
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Description

Thymulin Synthetic is a single, non-glycosylated polypeptide chain containing 9 amino acids, having a molecular mass of 858 Dalton and a Molecular formula of C33H54N12O15.

Formulation

The protein was lyophilized with no additives.

Purity

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

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Thymulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymulin 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 Thymulin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Pyr-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn-OH.
Background
Thymulin, a nonapeptide hormone, is produced primarily by the thymus gland and has been recognized for its pivotal role in the immune system. It plays a significant role in the maturation and differentiation of T lymphocytes, which are crucial for immune function. Beyond its immune-related functions, research has increasingly unveiled the diverse physiological roles of thymulin. This study aims to comprehensively investigate thymulin, shedding light on its immunological functions and exploring its potential applications in various aspects of health and medicine.
The primary objective of this research is to elucidate the mechanisms underlying thymulin's role in immune regulation. In vitro and in vivo experiments will be conducted to explore thymulin's interactions with immune cells, its impact on T cell development and function, and its potential modulation of immune responses. Understanding these mechanisms is fundamental for harnessing thymulin's immunomodulatory properties.
The second objective is to assess the clinical relevance of thymulin in immune-related disorders. Clinical trials and studies involving individuals with autoimmune diseases, immunodeficiencies, and age-related immune decline will be conducted to evaluate the potential therapeutic applications of thymulin. These investigations may offer insights into the use of thymulin as an immunomodulatory agent in various clinical settings.
The third objective is to explore the broader implications of thymulin in health and medicine. Research will investigate its potential roles in areas beyond immunology, such as neuroprotection, wound healing, and tissue regeneration. Understanding the multifaceted properties of thymulin may open new avenues for therapeutic interventions in various medical specialties.
By delving into the diverse functions of thymulin, this research aims to expand our knowledge of its physiological roles and clinical applications. The findings may have implications for the development of innovative approaches in immunology and healthcare, ultimately benefiting patients affected by immune-related disorders and other medical conditions.
What is the molecular weight/Mw of THYMALIN Protein?
THYMALIN Protein has a total Mw of 0.85kDa.

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

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

What is the amino acid sequence of THYMALIN Protein?
Pyr-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn-OH.

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

What is the endotoxin level for THYMALIN Protein?
The endotoxin level is minimal, THYMALIN 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:

Atosiban

Product # :

HOR-239

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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formulation
purity
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HPLC, MS
Citations

Description

Atosiban also called ADH (Anti-Diuretic Hormone) has a molecular formula of C43H67N11O12S2, 3-Mercaptopropionyl-D-Tyr(ET)-Ile-Thr-Asn-Cys-Pro-Orn-Gly-NH2 having a Mw of 994.2 Dalton.

Formulation

The Atosiban peptide was lyophilized with no additives.

Purity

Greater than 98.0% as determined by analysis by RP-HPLC.

HPLC, MS

More Info

Introduction
Atosiban is the first oxytocin antagonist to be specifically developed for the treatment of preterm labor. Atosiban has a specific mode of action, inhibiting oxytocin-induced uterine contractions by blocking oxytocin receptors in the uterus. Extensive clinical investigations have shown Atosiban to be at least as effective as current tocolytic agents. In addition, due to its novel and specific mode of action, Atosiban has a markedly improved maternal side effects profile compared with conventional therapies.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Atosiban although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Atosiban 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 Atosiban in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
What is the molecular weight/Mw of ATOSIBAN Protein?
ATOSIBAN Protein has a total Mw of 0.99kDa.

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

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

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

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

Who supplies ATOSIBAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of ATOSIBAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

SELANK

Product # :

HOR-035

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

SELANK Synthetic is a single, non-glycosylated polypeptide chain containing 7 amino acids, having a molecular mass of 751.89 Dalton and a Molecular formula of C33H57N11O9.

Formulation

The protein was lyophilized with no additives.

Purity

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

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SELANK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SELANK 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 SELANK 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-Thr-Lys-Pro-Arg-Pro-Gly-Pro-OH.
Background
Selank, also known as TP-7, is a synthetic peptide that has garnered significant attention in the scientific community due to its potential anxiolytic, neuroprotective, and nootropic effects. This heptapeptide, derived from the naturally occurring human tetrapeptide Tuftsin, has been shown to possess a wide range of biological activities, including enhancing memory, reducing anxiety, and potentially mitigating the effects of neurodegenerative diseases.
Selank's primary mechanism of action involves its interaction with the GABAergic system, the body's main inhibitory neurotransmitter system. By modulating the activity of GABA receptors, Selank can exert a calming effect on the brain, reducing anxiety and enhancing cognitive function. Studies by Semenova et al. (2014) have demonstrated that Selank can enhance memory and learning in rats, suggesting potential applications in cognitive enhancement and the treatment of cognitive disorders.
In addition to its anxiolytic and nootropic effects, Selank has been shown to possess neuroprotective properties. Research by Ershov et al. (2016) found that Selank could protect neurons from oxidative stress, suggesting potential applications in the treatment of neurodegenerative diseases such as Alzheimer's and Parkinson's disease.
Given its anxiolytic, nootropic, and neuroprotective effects, Selank has been proposed as a potential therapeutic agent for a variety of conditions, including anxiety disorders, cognitive disorders, and neurodegenerative diseases. For instance, a study by Medvedev et al. (2017) found that Selank could improve symptoms in patients with generalized anxiety disorder, indicating its potential as a therapeutic agent in the treatment of anxiety disorders.
While research on Selank is promising, it is important to note that most studies have been conducted in animals or in vitro. More research is needed to fully understand the potential effects and applications of Selank in humans. However, the existing body of research suggests that Selank could be a promising tool in the treatment of anxiety disorders, cognitive disorders, and neurodegenerative diseases.

What is the molecular weight/Mw of SELANK Protein?
SELANK Protein has a total Mw of 0.751kDa.

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

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

What is the amino acid sequence of SELANK Protein?
H-Thr-Lys-Pro-Arg-Pro-Gly-Pro-OH.

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

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

Who supplies SELANK that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of SELANK?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

Corticotropin Releasing Hormone Binding Protein (22-322 a.a.) Human Recombinant

Corticotropin releasing hormone binding protein, CRF-BP, CRH-BP, CRF-binding protein.

Product # :

HOR-025

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
purity
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Description

CRHBP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (22-322 a.a) and having a molecular mass of 36.1kDa.CRHBP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CRHBP protein (1mg/ml) contains 10% glycerol, 0.4M urea and 20mM Tris-HCl buffer (pH 8.0).

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
Corticotropin Releasing Hormone Binding Protein or CRHBP is a hormone that stimulates the preopiomelanocortin-derived peptides secretion & synthesis. In general, the levels of CRHBP in the human plasma are relatively low. There are times when we can find high levels of the hormone, mainly in pregnancy, after parturition the levels drop back, the high levels are thought to be derived from the placenta. CRH-binding protein can be found in the plasma, this protein inactivates CRH, in order to avoid inappropriate pituitary-adrenal stimulation during gestation.
Synonyms
Corticotropin releasing hormone binding protein, CRF-BP, CRH-BP, CRF-binding protein.
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 MGSESRYLEL REAADYDPFL LFSANLKREL AGEQPYRRAL RCLDMLSLQG QFTFTADRPQ LHCAAFFISE PEEFITIHYD QVSIDCQGGD FLKVFDGWIL KGEKFPSSQD HPLPSAERYI DFCESGLSRR SIRSSQNVAM IFFRVHEPGN GFTLTIKTDP NLFPCNVISQ TPNGKFTLVV PHQHRNCSFS IIYPVVIKIS DLTLGHVNGL QLKKSSAGCE GIGDFVELLG GTGLDPSKMT PLADLCYPFH GPAQMKVGCD NTVVRMVSSG KHVNRVTFEY RQLEPYELEN PNGNSIGEFC LSGL

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:

Exenatide

Exendin-4.

Product # :

HOR-246

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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formulation
purity
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Description

Exenatide is a single, non-glycosylated, peptide containing 39 amino acids and having a molecular mass of 4186.6 Dalton. Exenatide has the empirical formula C184H282N50O60S.

Formulation

The Exenatide peptide was lyophilized from a concentrated solution with no additives.

Purity

Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

More Info

Introduction
Exenatide Derived from the saliva of the gila monster, is a 39 amino acid peptide that mimics the GLP-1 incretin, an insulin secretagogue with glucoregulatory effects. Typical responses to exenatide include improvements in the initial rapid release of endogenous insulin, suppression of glucagon release by the pancreas, regulation of gastric empyting, and reduced appetite - all of which function to lower blood glucose. Exenatide is self-regulating in that it lowers blood sugar when levels are elevated but does not continue to lower blood sugar when levels return to normal, unlike with sulfonylureas or insulins.
Synonyms
Exendin-4.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Exenatide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Exenatide 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 Exenatide 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-His-Gly-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Leu-Ser-Lys-Gln-Met-Glu-Glu-Glu-Ala-Val-Arg-Leu-Phe-Ile-Glu-Trp-Leu-Lys-Asn-Gly-Gly-Pro-Ser-Ser-Gly-Ala-Pro-Pro-Pro-Ser-NH2.
Background
What is the molecular weight/Mw of EXENATIDE Protein?
EXENATIDE Protein has a total Mw of 4.18kDa.

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

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

What is the amino acid sequence of EXENATIDE Protein?
H-His-Gly-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Leu-Ser-Lys-Gln-Met-Glu-Glu-Glu-Ala-Val-Arg-Leu-Phe-Ile-Glu-Trp-Leu-Lys-Asn-Gly-Gly-Pro-Ser-Ser-Gly-Ala-Pro-Pro-Pro-Ser-NH2.

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

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

Who supplies EXENATIDE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of EXENATIDE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

Melanotan-I

Melanotan-I, MT-I, Melanotan-1.

Product # :

HOR-306

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
formulation
purity
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Citations

Description

Melanotan-I has the amino acid sequence of Ser-Tyr-Ser-Nle-Glu-His-D-Phe-Arg-Trp-Gly-Lys-Pro-Val and a molecular weight of 1647.4 Dalton.

Formulation

The protein (1mg/ml) was lyophilized with no additives.

Purity

Greater than 98.0% as determined by RP-HPLC.

More Info

Synonyms
Melanotan-I, MT-I, Melanotan-1.
Physical Appearance
Sterile Filtered off-White lyophilized (freeze-dried) powder.
Stability
Lyophilized Melanotan-I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MT-I 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 Melanotan-I in sterile 1% acetic acid not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Ser-Tyr-Ser-Nle-Glu-His-D-Phe-Arg-Trp-Gly-Lys-Pro-Val
Background
What is the molecular weight/Mw of MELANOTAN-1 Protein?
MELANOTAN-1 Protein has a total Mw of 1.647kDa.

What is the Purity of MELANOTAN-1 Protein?
MELANOTAN-1 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of MELANOTAN-1 Protein?
The biological functionality of MELANOTAN-1 Protein will be determined in the future.

What is the amino acid sequence of MELANOTAN-1 Protein?
Ser-Tyr-Ser-Nle-Glu-His-D-Phe-Arg-Trp-Gly-Lys-Pro-Val

What applications can MELANOTAN-1 Protein be used in?
MELANOTAN-1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for MELANOTAN-1 Protein?
The endotoxin level is minimal, MELANOTAN-1 Protein was purified using conventional chromatography techniques.

Who supplies MELANOTAN-1 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of MELANOTAN-1?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

Cholinergic Receptor Nicotinic, Alpha 6 Human Recombinant

CHNRA6, Neuronal acetylcholine receptor subunit alpha-6, CHRNA6.

Product # :

PRO-1878

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
purity
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Description

CHRNA6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (26-239 a.a) and having a molecular mass of 29.3kDa. CHRNA6 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CHRNA6 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
Cholinergic Receptor Nicotinic, Alpha 6 (CHRNA6) is a part of the nicotinic acetylcholine receptors (nAChRs) family. nAChRs are heteropentameric ligand-gated ion channels generating from the assembly of alpha and beta protein subunits. After binding acetylcholine, the AChRs respond by a major change in conformation which affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. CHRNA6 receptors have a rather selective localization to the nigrostriatal pathway.
Synonyms
CHNRA6, Neuronal acetylcholine receptor subunit alpha-6, CHRNA6.
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 KDRWGSKGCV GCATEERLFH KLFSHYNQFI RPVENVSDPV TVHFEVAITQ LANVDEVNQI METNLWLRHI WNDYKLRWDP MEYDGIETLR VPADKIWKPD IVLYNNAVGD FQVEGKTKAL LKYNGMITWT PPAIFKSSCP MDITFFPFDH QNCSLKFGSW TYDKAEIDLL IIGSKVDMND FWENSEWEII DASGYKHDIK YNCCEEIYTD ITYSFYIRRL.

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:

Lanreotide

Product # :

HOR-282

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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formulation
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Description

Lanreotide is an octapeptide, an analogue of a naturally occurring hormone, somatostatin.

Formulation

The protein (1mg/ml) was lyophilized with 5mg manntitol and 0.04mg tween-80.

Purity

Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

More Info

Introduction
Lanreotide is a peptide inhibitor of a number of endocrine, neuroendocrine, exocrine and paracrine functions. It shows good affinity for peripheral somatostatin receptors (anterior pituitary and pancreatic). In contrast, its affinity for central receptors is much lower. This profile confers a good specificity of action at the level of growth hormone and digestive hormone secretion. Lanreotide shows a much longer duration of action than natural somatostatin. In addition, its marked selectivity for the secretion of growth hormone, compared to that of insulin, makes it a suitable candidate for the treatment of acromegaly. By inhibiting the synthesis of thyroid stimulating hormone (TSH), lanreotide also normalised thyroid function of patients with thyrotrophin secreting adenomas in 50% (8/16) of the per-protocol population treated for 6 months. There was no significant reduction in the size of the adenoma. Furthermore, the inhibitory action of lanreotide on intestinal exocrine secretion, d
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Lanreotide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Lanreotide 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 Lanreotide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Background
What is the Purity of LANREOTIDE Protein?
LANREOTIDE Protein is >99% pure as determined by SDS-PAGE.

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

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

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

Who supplies LANREOTIDE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of LANREOTIDE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

Thyrostimulin Alpha Human Recombinant

GPA2, GPHA2, ZSIG51, Glycoprotein hormone alpha-2, MGC126572.

Product # :

HOR-258

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Quantity :

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Shipped at Room temp

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Description

GPHA2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 120 amino acids and having a total molecular mass of 13.28 kDa. The Thyrostimulin contains His tag which consists of 14 additional amino acids.The amino acid sequence of the recombinant human Thyrostimulin beta subunit is 100% homologous to the amino acid sequence of the human Thyrostimulin beta subunit without signal sequence. (N-terminal 24AA).Thyrostimulin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GPHA2 filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M Acetate buffer pH 4.

Purity

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

More Info

Introduction
Human thyrostimulin ranks among the glycoprotein hormone family. These hormones consist of two subunits, the common alpha- and specific beta-subunits, which associate noncovalently to form a heterodimer. The alpha-subunit combines with four distinct beta-subunits giving rise to four biologically active hormones in human: FSH, LH, TSH, and CG. FSH, LH, and TSH, mainly expressed in the anterior pituitary, are essential for coordinated endocrine regulation in the hypothalamus- pituitary axis and show to activate specific G protein–coupled receptors in the thyroid (TSH receptor) and gonads (LH and FSH receptors), respectively.
The heterodimeric glycoprotein hormones have only been identified in vertebrates and are highly conserved in organisms from primitive rayfin fish (Chondrostei) to human in both primary sequences and functional characteristics.
Corticotroph-derived glycoprotein hormone (CGH), also referred to as thyrostimulin, is a noncovalent heterodimer of glycoprotein hormone alpha 2 (GPHA2) and glycoprotein hormone beta 5 (GPHB5).
Recombinant A2/B5 heterodimeric glycoproteins activates human TSH receptors, but not LH and FSH receptors, and shows high affinity to TSH receptors in a radioligand receptor assay. The heterodimer also stimulates cAMP production and thymidine incorporation by cultured thyroid cells and increases serum thyroxine levels in TSH-suppressed rats in vivo. This new heterodimeric glycoprotein hormone was named as thyrostimulin based on its thyroid-stimulating activity. The expression of thyrostimulin in the anterior pituitary known to express TSH receptors suggested a paracrine mechanism.
Synonyms
GPA2, GPHA2, ZSIG51, Glycoprotein hormone alpha-2, MGC126572.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Thyrostimulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GPHA2 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 add 0.1M Acetate buffer pH4 to prepare a working stock solution of ~ 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 protein 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 GMAS QEAVIPG CHLHPFNVTV RSDRQGTCQG SHVAQACVGH CESSAFPSRY SVLVASGYRH NITSVSQCCT ISGLKKVKVQ LQCVGSRREE LEIFTARACQCDMCRLSRY.
Background
What is the molecular weight/Mw of GPHA2 Protein?
GPHA2 Protein has a total Mw of 13.28kDa.

What is the source or expression system of GPHA2 Protein?
Escherichia Coli.

What is the Purity of GPHA2 Protein?
GPHA2 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GPHA2 Protein?
The biological functionality of GPHA2 Protein will be determined in the future.

What is the amino acid sequence of GPHA2 Protein?
MRGSHHHHHH GMAS QEAVIPG CHLHPFNVTV RSDRQGTCQG SHVAQACVGH CESSAFPSRY SVLVASGYRH NITSVSQCCT ISGLKKVKVQ LQCVGSRREE LEIFTARACQCDMCRLSRY.

What applications can GPHA2 Protein be used in?
GPHA2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GPHA2 Protein?
The endotoxin level is minimal, GPHA2 Protein was purified using conventional chromatography techniques.

Who supplies recombinant GPHA2 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of GPHA2?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

Cetrorelix

Product # :

HOR-277

Price :

Quantity :

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Shipped at Room temp

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Description

Cetrorelix acetate is a synthetic decapeptide with gonadotropin-releasing hormone (GnRH) antagonistic activity. Cetrorelix acetate is an analog of native GnRH with substitutions of amino acids at positions 1, 2, 3, 6, and 10. The molecular formula is C70H92CIN17O14 (Ac-D-Nal1-D-Cpa2-D-Pal3-Ser4-Tyr5- D-Cit6-Leu7-Arg8-Pro9-D -Ala10-NH2), and the molecular weight is 1431 Dalton, calculated as the anhydrous free base.

Formulation

The Cetrorelix peptide was lyophilized with no additives.

Purity

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

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Cetrorelix although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Cetrorelix 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 Cetrorelix in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Background
What is the molecular weight/Mw of CETRORELIX Protein?
CETRORELIX Protein has a total Mw of 1.4kDa.

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

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

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

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

Who supplies CETRORELIX that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CETRORELIX?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

Goserelin

Product # :

HOR-256

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Goserelin contains 10 amino acids Glu1-His2-Trp3-Ser4-Tyr5-D-Ser(tBu)6-Leu7-Arg8-Pro9-AzGly10-NH2 and having a molecular weight of 1269.43 Dalton.

Formulation

The protein (1 mg/ml) was lyophilized with no additives.

Purity

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

More Info

Introduction
Goserelin is a hormone similar to the one normally released from the hypothalamus gland in the brain (GnRH super-agonist). It is used to treat for prostate and breast cancer.
Goserelin decreases the amount of estrogen and testosterone by this treating endometriosis and cancer of the breast, and can help thin the uterus lining before surgery. Goserelin prevents the growth of tissue associated with endometriosis.
Reducing the amount of testosterone is one way of treating prostate cancer.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Goserelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Goserelin 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 Goserelin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Background
What is the molecular weight/Mw of GOSERELIN Protein?
GOSERELIN Protein has a total Mw of 1.269kDa.

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

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

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

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

Who supplies GOSERELIN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of GOSERELIN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

Ornipressin

Product # :

HOR-036

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Ornipressin Synthetic is a single, non-glycosylated polypeptide chain containing 9 amino acids, having a molecular mass of 1042.19 Dalton and a Molecular formula of C45H63N13O12 S2.

Formulation

The protein was lyophilized with no additives.

Purity

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

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Ornipressin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Ornipressin 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 Ornipressin 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-Cys-Tyr-Phe-Gln-Asn-Cys-Pro-Orn-Gly-NH2.
Background
Ornipressin, a naturally occurring non-mammalian vasopressin analogue, has been recognized for its role in vasoconstriction and antidiuresis, making it an invaluable agent in certain clinical settings (Holmes et al., 2003). This paper aims to comprehensively review ornipressin's biochemical properties, its clinical applications, and potential future directions for therapeutic use.
Ornipressin is characterized by its strong vasopressin V1 receptor agonist activity, resulting in intense vasoconstriction. It also exhibits antidiuretic properties through the activation of V2 receptors in the renal collecting ducts, albeit to a lesser extent compared to vasopressin (Evans & Davidson, 1964).
Clinical applications of ornipressin are mainly driven by its potent vasoconstrictor activity. It has shown promise in managing esophageal variceal bleeding, where its vasoconstrictive properties help achieve hemostasis (Bosch et al., 2004).
Furthermore, it has been used as a rescue therapy in vasodilatory shock, where traditional vasoconstrictors may have limited effect (Morelli et al., 2005).
As our understanding of ornipressin continues to expand, future research is directed toward fine-tuning its application in various clinical scenarios and exploring potential new therapeutic roles. Current research is investigating the possible neuroprotective role of ornipressin in conditions such as cerebral ischemia (Uchida et al., 2010).
Ornipressin, with its robust vasoconstrictor and antidiuretic properties, plays a crucial role in managing certain clinical situations. As we continue to explore this intriguing compound, its therapeutic potential appears to be far-reaching, warranting continued research in this field.

What is the molecular weight/Mw of ORNIPRESSIN Protein?
ORNIPRESSIN Protein has a total Mw of 1.042 kDa.

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

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

What is the amino acid sequence of ORNIPRESSIN Protein?
H-Cys-Tyr-Phe-Gln-Asn-Cys-Pro-Orn-Gly-NH2.

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

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

Who supplies ORNIPRESSIN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of ORNIPRESSIN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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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