Search: 1000 results found for "Chromogranin"

Description:

Delta Sleep Inducing Peptide

Product # :

HOR-030

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
formulation
purity
More Info
Citations

Description

DSIP Synthetic is a single, non-glycosylated polypeptide chain containing 15 amino acids, having a molecular mass of 1419.55 Dalton and a Molecular formula of C62H98N16O22.

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 DSIP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DSIP 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 DSIP 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-Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val-OH
Background
Delta Sleep-Inducing Peptide (DSIP), also known as Sleep-Promoting Peptide, is a neuropeptide that has been the subject of extensive research due to its potential role in sleep regulation, stress response, and neuroprotection. This nonapeptide, first isolated from the cerebral venous blood of rabbits during sleep, has been shown to induce slow-wave sleep, modulate pain perception, and exhibit potential antioxidant and immunomodulatory properties.
DSIP's primary function is its interaction with the sleep regulatory system. By modulating the release of certain neurotransmitters, DSIP can influence sleep patterns, particularly promoting slow-wave sleep, the most restorative stage of sleep. Studies by Kovalzon et al. (2011) have demonstrated that DSIP can enhance sleep quality in rats, suggesting potential applications in sleep disorders and the promotion of healthy sleep patterns.
In addition to its sleep-inducing effects, DSIP has been shown to possess neuroprotective properties. Research by Zolotarev et al. (2014) found that DSIP 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 sleep-inducing and neuroprotective effects, DSIP has been proposed as a potential therapeutic agent for a variety of conditions, including sleep disorders, chronic pain, and neurodegenerative diseases. For instance, a study by Spong et al. (2016) found that DSIP could improve sleep quality in patients with chronic insomnia, indicating its potential as a therapeutic agent in the treatment of sleep disorders.
While research on DSIP 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 DSIP in humans. However, the existing body of research suggests that DSIP could be a promising tool in the treatment of sleep disorders, chronic pain, and neurodegenerative diseases.

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:

Buserelin

Product # :

HOR-255

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
formulation
purity
More Info
Citations

Description

Buserelin contains 9 amino acids Glu-His-Trp-Ser-Tyr-D-Ser(tBu)-Leu-Arg-Pro-NHEt and having a molecular weight of 1239.44 Dalton.

Formulation

The Buserelin 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

Introduction
Buserelin belongs to the group of gonadotrophin releasing hormone (gonadorelin) analogues (LHRH agonist). It acts on the pituitary gland which controls the amount of many different types of hormones (chemical messengers). It alters the amount of hormones, particularly the oestrogens androgens. This alteration of hormone levels can be exploited to treat cancers of the prostate gland, which are stimulated to grow by testosterone. Buserelin lowers the levels of testosterone, which starves the tumour of testosterone and causes it to shrink.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Buserelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Buserelin 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 Buserelin 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 BUSERELIN Protein?
BUSERELIN Protein has a total Mw of 1.24kDa.

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

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

What is the amino acid sequence of BUSERELIN Protein?
BUSERELIN Protein is composed from 9 amino acids.

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

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

Who supplies BUSERELIN 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 BUSERELIN?
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:

Sincalide

Product # :

HOR-274

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
formulation
purity
More Info
Citations

Description

Sincalide also called CCK-8 has a molecular formula of C49H62N10O16S3 , H-Asp-Tyr(SO3H)-Met-Gly-Trp-Met-Asp-Phe-NH2 having an Mw of 1143.29 Dalton.

Formulation

The Sincalide was lyophilized from a concentrated (1mg/ml) solution with no additives.

Purity

Greater than 99.0% as determined by RP-HPLC.

More Info

Introduction
Sincalide corresponds to the C-terminal octapeptide of cholecystokinin (CCK) which acts on receptors within the gallbladder wall causing it to contract.
Cholecystokinin (CCK) is a hormone originally isolated from porcine intestinal mucosa and described as a linear 33-amino acid peptide containing a sulfated tyrosine, which is essential for its biological activity. It has been found in mammals in both the digestive tract and the central nervous system. Among its multiple biological functions, this hormone stimulates pancreatic exocrine secretion, gallbladder contraction, and intestine motility and may also act as a neurotransmitter/neuromodulator in the central nervous system.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Sincalide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCK-8 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 Sincalide in sterile 18MΩ-cm H2O at a concentration of 0.5mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-Asp-Tyr(SO3H)-Met-Gly-Trp-Met-Asp-Phe-NH2
Background
What is the molecular weight/Mw of SINCALIDE Protein?
SINCALIDE Protein has a total Mw of 1.143kDa.

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

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

What is the amino acid sequence of SINCALIDE Protein?
H-Asp-Tyr(SO3H)-Met-Gly-Trp-Met-Asp-Phe-NH2

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

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

Who supplies SINCALIDE 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 SINCALIDE?
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:

Recombinant Human Tamm Horsfall Glycoprotein

Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.

Product # :

ENZ-1206

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
SDS-PAGE
Citations

Description

Uromodulin Human Recombinant protein produced from HEK Cells, is a polypeptide chain containing 595 amino acids ( 25-613 a.a. ) and having a total Mw of 65 kDa. Uromodulin is expressed with a 6 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

HEK293

Formulation

The UMOD protein was lyophilized from 0.4μm filtered solution containing 50mM NaCl, 0.02M TRIS, pH 7.5.

Purity

Greater than 90.0% as determined by SDS-PAGE analysis.

SDS-PAGE

More Info

Introduction
Uromodulin (Tamm–Horsfall protein) is produced mainly by cells in the kidney’s thick ascending limb and is the most abundant protein in normal urine.
Uromodulin takes part in salt and water regulation, helps prevent urinary tract infections and kidney stones, and influences inflammation and immune activity in the kidney.
Reduced Uromodulin levels is associated with chronic kidney disease.
UMOD mutations causes unproper protein folding and thus transported incorrectly, resulting in its accumulation inside kidney tubular cells that damages the tubules and cause kidney disease (ADTKD-UMOD), associated with high uric acid, gout, and progressive kidney failure.
Synonyms
Tamm-Horsfall urinary glycoprotein, THP, FJHN, HNFJ, THGP, MCKD2, ADMCKD2, UMOD, Uromodulin.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized UMOD although stable at room temperature for 3 weeks, should be stored at -18C. Upon reconstitution UMOD 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
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 in the cell culture.
Amino Acid Sequence
DTSEARWCSE CHSNATCTED EAVTTCTCQE GFTGDGLTCV DLDECAIPGA HNCSANSSCV NTPGSFSCVC PEGFRLSPGL GCTDVDECAE PGLSHCHALA TCVNVVGSYL CVCPAGYRGD GWHCECSPGS CGPGLDCVPE GDALVCADPC QAHRTLDEYW RSTEYGEGYA CDTDLRGWYR FVGQGGARMA ETCVPVLRCN TAAPMWLNGT HPSSDEGIVS RKACAHWSGH CCLWDASVQV KACAGGYYVY NLTAPPECHL AYCTDPSSVE GTCEECSIDE DCKSNNGRWH CQCKQDFNIT DISLLEHRLE CGANDMKVSL GKCQLKSLGF DKVFMYLSDS RCSGFNDRDN RDWVSVVTPA RDGPCGTVLT RNETHATYSN TLYLADEIII RDLNIKINFA CSYPLDMKVS LKTALQPMVS ALNIRVGGTG MFTVRMALFQ TPSYTQPYQG SSVTLSTEAF LYVGTMLDGG DLSRFALLMT NCYATPSSNA TDPLKYFIIQ DRCPHTRDST IQVVENGESS QGRFSVQMFR FAGNYDLVYL HCEVYLCDTM NEKCKPTCSG TRFRSGSVID QSRVLNLGPI TRKGVQATVH HHHHH
Background
What is the function of Uromodulin?
Uromodulin is the most abundant protein in normal urine. Its secretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin plays a role as a constitutive inhibitor of calcium crystallization in renal fluids. Secretion of uromodulin in urine provides protection against urinary tract infections caused by uropathogenic bacteria. Defects in Uromodulin expression are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. UMOD is involved in regulating the circulating activity of cytokines as it binds to il-1, il-2 and tnf with high affinity.

What is the molecular weight/Mw of Uromodulin Protein?
UMOD Protein has a total Mw of 65kDa.

What is the source or expression system of Uromodulin Protein?
HEK293.

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

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

What is the amino acid sequence of Uromodulin Protein?
UMOD Protein is composed from 595 amino acids.

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

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

RAS-like, Estrogen-Regulated, Growth Inhibitor Human Recombinant

Ras-related and estrogen-regulated growth inhibitor, RERG, MGC15754.

Product # :

PRO-106

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

RERG Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 219 amino acids (1-199 a.a.) and having a molecular mass of 24.7kDa (Molecular size on SDS-PAGE will appear higher). The RERG is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The RERG solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 50% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
RERG is a 199 amino acid protein which localizes in the cytoplasm and is a member of the Ras subfamily of small GTPases. RERG is expressed in the pancreas, liver, skin, lung, brain, kidney and heart tissue. RERG is a vital mediator of diverse cell signaling pathways, including those leading to cell proliferation, cytoskeletal organization and secretion.
Synonyms
Ras-related and estrogen-regulated growth inhibitor, RERG, MGC15754.
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 MAKSAEVKLA IFGRAGVGKS ALVVRFLTKR FIWEYDPTLE STYRHQATID DEVVSMEILD TAGQEDTIQR EGHMRWGEGF VLVYDITDRG SFEEVLPLKN ILDEIKKPKN VTLILVGNKA DLDHSRQVST EEGEKLATEL ACAFYECSAC TGEGNITEIF YELCREVRRR RMVQGKTRRR SSTTHVKQAI NKMLTKISS.

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:

Energy Homeostasis Associated Human Recombinant

Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.

Product # :

PRO-1569

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

ENHO Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 34-76) containing 121 amino acids including extra 78 N-terminal amino acids. The total molecular mass is 13.05kDa (calculated).

Source

Escherichia Coli.

Formulation

ENHO filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Energy Homeostasis Associated (ENHO) participates in glucose homeostasis maintenance and lipid metabolism. ENHO is expressed in the liver and the brain. The role of ENHO in obesity or diabetes is studied.
Synonyms
Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.
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 deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. ENHO is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MGGKSNGEKK YIVGFKQGFK SCAKKEDVIS EKGGKLQKCF KYVDAASATL NEKAVEELKK DPSVAYVEED KLFKALTSCHSRSADVDSLS ESSPNSSPGP CPEKAPPPQK PSHEGSYLLQ P.

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 E/M, BioActive Human Recombinant

Cystatin E/M, cystatin 6, Cystatin M, Cystatin-E, Cysteine proteinase inhibitor.

Product # :

PRO-2633

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

CST6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 142 amino acids (29-149 a.a.) and having a molecular mass of 15.9kDa.CST6 is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The CST6 solution (0.5mg/1ml) contains 10% glycerol, 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The IC50 value is < 10nM. The inhibitory function of Cystatin 6 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25˚C.

More Info

Introduction
Cystatin E/M or CST6 is part of the cystatin type 2 family. Part of the cystatin type 2 family members can act as cysteine protease inhibitors, whereas cystatin E/M regulates cathepsin B inhibitors and not cathepsin C. cystatin E/M is a protein the when secreted, has an effect on osteogenesis and bone resorption, insulin regulation, response to systemic inflammation & hepatocyte growth factor receptors.
Synonyms
Cystatin E/M, cystatin 6, Cystatin M, Cystatin-E, Cysteine proteinase inhibitor.
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 MRPQERMVGE LRDLSPDDPQ VQKAAQAAVA SYNMGSNSIY YFRDTHIIKA QSQLVAGIKY FLTMEMGSTD CRKTRVTGDH VDLTTCPLAA GAQQEKLRCD FEVLVVPWQN SSQLLKHNCV QM

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:

Casein Kinase 1 alpha 1 Human Recombinant

Casein kinase I isoform alpha, CKI-alpha, CK1, CSNK1A1, HLCDGP1, PRO2975.

Product # :

PKA-056

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

CSNK1A1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-337) and having a molecular mass of 41kDa. CSNK1A1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The CSNK1A1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 80% as determined by SDS-PAGE.

More Info

Introduction
Caseine Kinase 1 alpha belongs is a member of the protein kinase superfamily, CK1 Ser/Thr protein kinase family, Casein kinase I subfamily. The CK1 isoforms - alpha, beta, gamma, delta, epsilon and their splice variants are involved in diverse cellular processes including membrane trafficking, circadian rhythm, cell cycle progression, chromosome segregation, apoptosis and cellular differentiation. Possibly CSNK1A1 can phosphorylate a large number of proteins and is involved in Wnt signaling where it phosphorylates CTNNB1 on Ser45. CSNK1A1 also interacts with the Axin complex.
Synonyms
Casein kinase I isoform alpha, CKI-alpha, CK1, CSNK1A1, HLCDGP1, PRO2975.
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 MASSSGSKAE FIVGGKYKLV RKIGSGSFGD IYLAINITNG EEVAVKLESQ KARHPQLLYE SKLYKILQGG VGIPHIRWYG QEKDYNVLVM DLLGPSLEDL FNFCSRRFTM KTVLMLADQM ISRIEYVHTK NFIHRDIKPD NFLMGIGRHC NKLFLIDFGL AKKYRDNRTR QHIPYREDKN LTGTARYASI NAHLGIEQSR RDDMESLGYV LMYFNRTSLP WQGLKAATKK QKYEKISEKK MSTPVEVLCK GFPAEFAMYL NYCRGLRFEE APDYMYLRQL FRILFRTLNH QYDYTFDWTM LKQKAAQQAA SSSGQGQQAQ TPTGKQTDKT KSNMKGF.

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-b4 Human Recombinant

Thymosin beta-4, T beta 4, Fx , TB4X, PTMB4, TMSB4.

Product # :

HOR-003

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

Thymosin b4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 43 amino acids and having a molecular mass of 4.9kDa.The Thymosin b4 Human is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2um filtered concentrated solution in 1xPBS, pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.

More Info

Introduction
CB1 cannabinoid receptor-interacting protein 1 (CNRIP1) is a 164 amino acid protein and G-protein coupled receptor which is a member of the CNRIP family. The CNRIP1 interacts with the C-terminal tail of cannabinoid receptor 1. CNRIP1 is expressed in the brain tissue and, at low levels, in the testis. CNRIP1 is involved in appetite, synaptic plasticity, neuroprotection and analgesia.
Synonyms
Thymosin beta-4, T beta 4, Fx , TB4X, PTMB4, TMSB4.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Thymosin B4 Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymosin B4 Human 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 Thymosin B4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SDKPDMAEIE KFDKSKLKKT ETQEKNPLPS KETIEQEKQA GES
Background
What is the molecular weight/Mw of THYMOSIN BETA 4 HUMAN Protein?
THYMOSIN BETA 4 HUMAN Protein has a total Mw of 4.9kDa.

What is the source or expression system of THYMOSIN BETA 4 HUMAN Protein?
Escherichia Coli.

What is the Purity of THYMOSIN BETA 4 HUMAN Protein?
THYMOSIN BETA 4 HUMAN Protein is >95% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of THYMOSIN BETA 4 HUMAN Protein?
SDKPDMAEIE KFDKSKLKKT ETQEKNPLPS KETIEQEKQA GES

What applications can THYMOSIN BETA 4 HUMAN Protein be used in?
THYMOSIN BETA 4 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

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

Who supplies recombinant THYMOSIN BETA 4 HUMAN 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 HUMAN?
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:

Insulin (20-110 a.a) Human Recombinant

Product # :

CYT-1237

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

The Insulin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Insulin His-Tagged Fusion Protein, produced in E. coli, is a 13kDa protein containing 91 amino acid residues of the Insulin Human, 20-110 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.

More Info

Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized Insulin 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.
Amino Acid Sequence
MALWMRLLPL LALLALWGPD PAAAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN
Background
Insulin participates in the metabolism of carbohydrates, proteins and fats by regulating glucose homeostasis in the body. Insulin decreases blood glucose concentration. Insulin hormone facilitates the uptake of glucose into cells, mainly in muscle and fat tissues, and stimulates the liver to store glucose as glycogen. Insulin also inhibits the production of gluconeogenesis and promotes the synthesis of proteins and lipids. Insulin increases cell permeability to monosaccharides, fatty acids and amino acids. Insulin accelerates glycolysis, the pentose phosphate cycle and glycogen synthesis in liver.

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:

Crystallin, Gamma D Mouse Recombinant

Gamma-crystallin D, Gamma-D-crystallin , Gamma-crystallin 1, CRYGD.

Product # :

PRO-2484

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

CRYGD Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (1-174 a.a.) and having a molecular mass of 23.5kDa.CRYGD is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CRYGD protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
CRYGD is a member of the beta/gamma-crystallin family. Crystallins are the principal structural components of the vertebrate eye lens. The mammalian lens crystallins are divided into alpha, beta, and gamma families. Gamma-crystallins are involved in cataract formation. Defects in the CRYGD gene are responsible for cataract autosomal dominant (ADC), cataract congenital non-nuclear polymorphic autosomal dominant (CCP), cataract congenital cerulean type 3 (CCA3) and cataract crystalline aculeiform (CACA).
Synonyms
Gamma-crystallin D, Gamma-D-crystallin , Gamma-crystallin 1, CRYGD.
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 MGSMGKITFY EDRGFQGRHY ECSTDHSNLQ PYFSRCNSVR VDSGCWMLYE QPNFTGCQYF LRRGDYPDYQ QWMGFSDSVR SCRLIPHAGS HRIRLYEREE YRGQMIEFTE DCPSLQDRFH FNEIYSLNVL EGCWVLYDMT NYRGRQYLLR PGEYRRYHDW
GAMNARVGSL RRVMDFY

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:

Tachykinin-3 Human Recombinant

Tachykinin-3, ZNEUROK1, Neurokinin-B, NKB, Neuromedin-K, TAC3, NKNB, PRO1155.

Product # :

PRO-716

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

TAC3 Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (17-121 a.a.) and having a molecular mass of 13.8kDa.The TAC3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TAC3 solution contains 20mM Tris-HCl buffer (pH 8.0) and 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Tachykinin-3 belongs to the substance P-related tachykinin family. Tachykinins are active peptides that stimulate neurons, induce behavioral responses, are effective vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. TAC3 and its receptor are essential switches of regulator of human puberty, regulated by the brain through the release of the GnRH which starts a chain of processes which eventually lead to the production of sex hormones.
During pregnancy, the expression of TAC3 is restricted to the outer syncytiotrophoblast of the placenta, significant concentrations of TAC3 can be identified in plasma as early as week 9, and plasma concentrations of TAC3 are grossly elevated in pregnancy-induced hypertension and pre-eclampsia. Higher Tachykinin-3 concentrations in normotensive pregnant women may be caused by the advanced gestational age and/or the result of a negative interaction of other vasoactive substances. TAC3 has a role in the continuance of high placental blood flow in normal pregnancy.
Synonyms
Tachykinin-3, ZNEUROK1, Neurokinin-B, NKB, Neuromedin-K, TAC3, NKNB, PRO1155.
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 QSFGAVCKEP QEEVVPGGGR SKRDPDLYQL LQRLFKSHSS LEGLLKALSQ ASTDPKESTS PEKRDMHDFF VGLMGKRSVQ PDSPTDVNQE NVPSFGILKY PPRAE.

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:

Cellular Repressor of E1A-Stimulated Genes 1 Mouse Recombinant

Protein CREG1, Cellular repressor of E1A-stimulated genes 1, Creg1, Creg.

Product # :

PRO-2387

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

CREG1 Mouse Recombinant produced in E. coli is a single polypeptide chain containing 213 amino acids (32-220) and having a molecular mass of 24kDa. CREG1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The CREG1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.15M NaCl.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Cellular Repressor of E1A-Stimulated Genes 1 (CREG1) both activates and inhibits gene expression to stimulate cellular proliferation and hinder differentiation. CREG1 antagonizes transcriptional activation and cellular transformation by E1A. CREG1 shares partial sequence similarity with E1A and binds both the general transcription factor TBP and the tumor suppressor pRb in vitro. CREG1 contributes to the transcriptional control of cell growth and differentiation.
Synonyms
Protein CREG1, Cellular repressor of E1A-stimulated genes 1, Creg1, Creg.
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 MGSMRGGRDH GDWDVDRRLP PLPPREDGPR VARFVTHVSD WGSLATISTI KEVRGWPFAD IISISDGPPG EGTGEPYMYL SPLQQAVSDL QENPEATLTM SLAQTVYCRN HGFDPQSPLC VHIMMSGTVT KVNKTEEDYA RDSLFVRHPE MKHWPSSHNW FFAKLKISRI WVLDYFGGPK VVTPEEYFNV TLQ.

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:

Follicle Stimulating Hormone Human Recombinant, CHO

Follitropin subunit beta, Follicle-stimulating hormone beta subunit, FSH-beta, FSH-B, Follitropin beta chain, FSH.

Product # :

HOR-067

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

FSH Human Recombinant produced in CHO cells is heterodimeric, glycosylated, polypeptide chain transfected with two expression plasmids encoding the human FSH-alpha chain (Accession # P01215) containing 92 amino and human FSH beta chain containing 111 amino acids (Accession # P01225) having a Mw of 33 kDa.
FSH human recombinant is purified by proprietary chromatographic techniques.

Source

CHO Cells

Formulation

The recombinant FSH was lyophilized from 0.2µm filtered solution containing PBS, pH 7.4.

Purity

Greater than 97% by SDS-PAGE and SEC-HPLC analyses.

Biological Activity

Determined by calf testes membrane, binding characteristics to the testicular FSH receptor which was found to be 25-200 pg/mL.

More Info

Introduction
Follicle stimulating hormone (FSH) is a hormone synthesised and secreted by gonadotropes in the anterior pituitary gland. FSH and LH act synergistically in reproduction: In women, in the ovary FSH stimulates the growth of immature Graafian follicles to maturation. As the follicle grows it releases inhibin, which shuts off the FSH production. In men, FSH enhances the production of androgen-binding protein by the Sertoli cells of the testes and is critical for spermatogenesis. In both males and females, FSH stimulates the maturation of germ cells. In females, FSH initiates follicular growth, specifically affecting granulosa cells. With the concomitant rise in inhibin B FSH levels then decline in the late follicular phase. This seems to be critical in selecting only the most advanced follicle to proceed to ovulation. At the end of the luteal phase, there is a slight rise in FSH that seems to be of importance to start the next ovulatory cycle. Like its partner, LH, FSH release at the pituitary gland is controlled by pulses of gonadotropin-releasing hormone (GnRH). Those pulses, in turn, are subject to the estrogen feed-back from the gonads.
Synonyms
Follitropin subunit beta, Follicle-stimulating hormone beta subunit, FSH-beta, FSH-B, Follitropin beta chain, FSH.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized recombinant FSH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FSH 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 Follicle Stimulating Hormone in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
FSH subunit alpha: APDVQDCPECTLQENPFFSQPGAPILQCMGCCFSRAYPTPLR SKKTMLVQKNVTSESTCCVAKSYNRVTVMGGFKVENHTACHCSTCYYHKS.
FSH subunit beta: NSCELTNITIAIEKEECRFCISINTTWCAGYCYTRDLVYKDP ARPKIQKTCTFKELVYETVRVPGCAHHADSLYTYPVATQCHCGKCDSDSTDCTVRGLGPSYCSFGEMKE.
Background
What is the molecular weight/Mw of FOLLICLE STIMULATING HORMONE, CHO Protein?
FOLLICLE STIMULATING HORMONE, CHO Protein has a total Mw of 33kDa.

What is the source or expression system of FOLLICLE STIMULATING HORMONE, CHO Protein?
CHO Cells.

What is the Purity of FOLLICLE STIMULATING HORMONE, CHO Protein?
FOLLICLE STIMULATING HORMONE, CHO Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of FOLLICLE STIMULATING HORMONE, CHO Protein?
Determined by calf testes membrane, binding characteristics to the testicular FSH receptor which was found to be 25 200 pg/mL.

What is the amino acid sequence of FOLLICLE STIMULATING HORMONE, CHO Protein?
FSH subunit alpha: APDVQDCPECTLQENPFFSQPGAPILQCMGCCFSRAYPTPLR SKKTMLVQKNVTSESTCCVAKSYNRVTVMGGFKVENHTACHCSTCYYHKS.
FSH subunit beta: NSCELTNITIAIEKEECRFCISINTTWCAGYCYTRDLVYKDP ARPKIQKTCTFKELVYETVRVPGCAHHADSLYTYPVATQCHCGKCDSDSTDCTVRGLGPSYCSFGEMKE.

What applications can FOLLICLE STIMULATING HORMONE, CHO Protein be used in?
FOLLICLE STIMULATING HORMONE, CHO Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FOLLICLE STIMULATING HORMONE, CHO Protein?
The endotoxin level is minimal, FOLLICLE STIMULATING HORMONE, CHO Protein was purified using conventional chromatography techniques.

Who supplies recombinant FOLLICLE STIMULATING HORMONE, CHO 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 FOLLICLE STIMULATING HORMONE, CHO?
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:

Growth Hormone Carp Recombinant

GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.

Product # :

CYT-297

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Growth Hormone Carp Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 188 amino acids & having a molecular mass of 21,408 Dalton. Growth Hormone Carp is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GH Carp was lyophilized from a concentrated (1mg/ml) solution with 0.3% NaHCO3 adjusted to pH 8.

Purity

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

Biological Activity

Carp GH is biologically active in rat 3T3 F442A preadipocytes, though its activity is 15-fold lower compared to bovine GH, but it is equally potent in vivo in promoting carp growth (Fine et al.1993). Furthermore, carp GH forms 1:2 complex with the extra cellular domain of ovine growth hormone receptor.

More Info

Introduction
Growth-Hormone is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.
Synonyms
GH1, GH, GHN, GH-N, hGH-N,Pituitary growth hormone, Growth hormone 1, Somatotropin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Growth Hormone Carp recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Growth Hormone Carp 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 Growth Hormone Carp recombinant in sterile 18MΩ-cm H2O 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 found to be Ser-Asp-Asn-Gln-Arg.

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:

Streptavidin Recombinant

Product # :

PRO-791

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

Streptavidin Streptomyces Avidinii Recombinant produced in E.Coli. The molecular weight per tetramer is approximately 52kDa.

Source

Escherichia Coli.

Formulation

Lyophilized in 10mM potassium phosphate buffer pH 6.5.

Purity

Greater than 98.0% as determined by SDS-PAGE and HPLC.

More Info

Introduction
Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is widely used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Streptavidin is shipped at ambient temperature, upon arrival store at -20°C.
Solubility
It is recommended to reconstitute the lyophilized Streptavidin in sterile 18MΩ-cm H2O not less than 0.5mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAEAGITGTWYNQLGSTFIVTAGADGALTGTYESAVGNAESRYVLT
GRYDSAPATDGSGTALGWTVAWKNNYRNAHSATTWSGQYVGGA
EARINTQWLLTSGTTEANAWKSTLVGHDTFTKVKPSAAS.
Proteolytic Activity
< 10-3 U/mg protein (Azocoll, 25 °C, 24 h, pH 8.0).
Specific Activity
> 17U/mg (one unit binds 1 μg D-biotin).

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:

Desmopressin

Product # :

HOR-270

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
formulation
purity
More Info
Citations

Description

Desmopressin also called ADH (Anti-Diuretic Hormone) has a molecular formula of C46H64N14O12S2 , Mpr-Tyr-Phe-Gln-Asn-Cys-Pro-D-Arg-Gly-NH2 having a Mw of 1069.23 Dalton.

Formulation

The protein (1mg/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
Desmopressin is the first vasopressin analog with a very high and very specific antidiuretic effect, has been widely used for different therapeutic purposes and is believed to be partly responsible for the formation of memories learning and memory processes. Desmopressin increases urine concentration and decreases urine production. Desmopressin is used to prevent and control excessive thirst, urination, and dehydration.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Desmopressin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DDAVP 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 DDAVP 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 DDAVP Protein?
DDAVP Protein has a total Mw of 1.06kDa.

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

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

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

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

Who supplies DDAVP 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 DDAVP?
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:

Casein kinase I isoform alpha, Mouse Anti Human

Casein kinase I isoform alpha, CKI-alpha, CK1, CSNK1A1, HLCDGP1, PRO2975.

Product # :

ANT-442

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

formulation
More Info
Citations

Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

More Info

Introduction
Caseine Kinase 1 alpha belongs is a member of the protein kinase superfamily, CK1 Ser/Thr protein kinase family, Casein kinase I subfamily. The CK1 isoforms - alpha, beta, gamma, delta, epsilon and their splice variants are involved in diverse cellular processes including membrane trafficking, circadian rhythm, cell cycle progression, chromosome segregation, apoptosis and cellular differentiation. Possibly CSNK1A1 can phosphorylate a large number of proteins and is involved in Wnt signaling where it phosphorylates CTNNB1 on Ser45. CSNK1A1 also interacts with the Axin complex.
Synonyms
Casein kinase I isoform alpha, CKI-alpha, CK1, CSNK1A1, HLCDGP1, PRO2975.
Immunogen
Anti-human CSNK1A1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CSNK1A1 amino acids 1-337 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
Clone
PAT2E2AT.
Applications
CSNK1A1 antibody has been tested by ELISA and 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 dilution range for Western blot analysis is 1:1000 ~ 2000. 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.
Purification Method
CSNK1A1 antibody was purified from mouse ascitic fluids by protein-G 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.

Description:

Secretagogin Human Recombinant

SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, SECRET, DJ501N12.8, Secretagogin.

Product # :

PRO-599

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

SCGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-276 a.a.) and having a molecular mass of 34.2kDa. SCGN is fused to a 20 amino acid His tag at N-terminus and purified by standard chromatography techniques.

Source

Escherichia Coli.

Formulation

SCGN His-Tag (1mg/ml) protein is supplied in 20mM Tris HCl pH-8, 1mM DTT, 0.1M NaCl and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
SCGN is a secreted calcium-binding protein which is found in the cytoplasm. It is related to calbindin D-28K and calretinin. Secretagogin is involved in KCL-stimulated calcium flux and cell proliferation.
Secretagogin plays a role in human non-functional pituitary adenomas.
Synonyms
SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, SECRET, DJ501N12.8, Secretagogin.
Physical Appearance
Sterile Filtered colorless liquid formulation.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDSSREPTLG RLDAAGFWQV WQRFDADEKG YIEEKELDAF FLHMLMKLGT DDTVMKANLH KVKQQFMTTQ DASKDGRIRM KELAGMFLSE DENFLLLFRR ENPLDSSVEF MQIWRKYDAD SSGFISAAEL RNFLRDLFLH HKKAISEAKL EEYTGTMMKI FDRNKDGRLD LNDLARILAL QENFLLQFKM DACSTEERKR DFEKIFAYYD VSKTGALEGP EVDGFVKDMM ELVQPSISGV DLDKFREILL RHCDVNKDGK IQKSELALCL GLKINP.

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:

Kallikrein-10 Human Recombinant, Sf9

Kallikrein-Related Peptidase 10, KLK10, PRSSL1, NES1, Normal Epithelial Cell-Specific 1, Protease Serine-Like 1, Kallikrein 10, Breast Normal Epithelial Cell Associated Serine Protease, kallikrein-10, Protease, Serine-Like 1, EC 3.4.21.- , EC 3.4.21, EC 3.4.21.74.

Product # :

ENZ-1090

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

KLK10 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 252 amino acids (34-276 a.a) and having a molecular mass of 27.8kDa. KLK10 protein is fused to a 6 amino acid His-Tag at C-terminus and purified by standard chromatography.

Source

Sf9, Baculovirus cells.

Formulation

KLK10 protein solution (0.5mg/ml) contains 30% glycerol, 20mM Tris-HCl (pH 8.0), 0.15M NaCl & 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
Kallikrein-10 (KLK10) is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19. Kallikreins are a subgroup of serine proteases having various physiological functions. KLK10 is secreted and has a role in suppression of tumorigenesis in breast and prostate cancers.
Synonyms
Kallikrein-Related Peptidase 10, KLK10, PRSSL1, NES1, Normal Epithelial Cell-Specific 1, Protease Serine-Like 1, Kallikrein 10, Breast Normal Epithelial Cell Associated Serine Protease, kallikrein-10, Protease, Serine-Like 1, EC 3.4.21.- , EC 3.4.21, EC 3.4.21.74.
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
ADPALLPQND TRLDPEAYGS PCARGSQPWQ VSLFNGLSFH CAGVLVDQSW VLTAAHCGNK PLWARVGDDH LLLLQGEQLR RTTRSVVHPK YHQGSGPILP RRTDEHDLML LKLARPVVLG PRVRALQLPY RCAQPGDQCQ VAGWGTTAAR RVKYNKGLTC SSITILSPKE CEVFYPGVVT NNMICAGLDR GQDPCQSDSG GPLVCDETLQ GILSWGVYPC GSAQHPAVYT QICKYMSWIN KVIRSNHHHH HH.

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 Human Recombinant, His Tag

CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.

Product # :

CYT-477

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

GMCSF Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids fragment (18-144) and having a molecular mass of 18.98kDa with an amino-terminal hexahistidine tag. GM-CSF Human Recombinant His is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Granulocyte Macrophage Colony Stimulating Factor-His is supplied in 20mM Tris HCl (pH 8) and 50% glycerol.

Purity

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

More Info

Introduction
GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene 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. Granulocyte Macrophage Colony Stimulating Factor is a potent species-specific growth factor produced by a variety of cell types including T cells, B cells, macrophages, mast cells and endothelial cells. GM-CSF is produced in response to cytokine or immune stimulation and has been shown to stimulate the proliferation, maturation and function of hematopoietic cells.
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.
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. Please avoid freeze thaw cycles.
Background
What is the molecular weight/Mw of GM-CSF HUMAN, HIS Protein?
GM-CSF HUMAN, HIS Protein has a total Mw of 18.98kDa.

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

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

What is the Biological Activity of GM-CSF HUMAN, HIS Protein?
The biological functionality of GM-CSF HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of GM-CSF HUMAN, HIS Protein?
GM-CSF HUMAN, HIS Protein is composed from 127 amino acids.

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

What is the endotoxin level for GM-CSF HUMAN, HIS Protein?
The endotoxin level is minimal, GM-CSF HUMAN, HIS 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:

Granulocyte-Colony Stimulating Factor Pegylated Human Recombinant

CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

Product # :

CYT-018

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8kDa. The Pegylated G-CSF is produced by attaching a 20kDa methoxypolyethylene glycol propionaldehyde (mPEG-ALD) to the N-terminal amino acid of G-CSF giving a total molecular mass of 38.8kDa. G-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

G-CSF is supplied in solution (0.69mg/ml) containing 10mM Acetate Buffer (pH 4.0), and 0.004% Polysorbate 80.

Purity

Greater than 95.0% as determined by SEC-HPLC.

Biological Activity

The ED₅₀, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

More Info

Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Physical Appearance
Colorless, clear and transparent solution.
Stability
G-CSF PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in theirpackaging to protect from light until the time of use. Shaking and freezing should be avoided.
Background
What is the molecular weight/Mw of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein has a total Mw of 18.8kDa.

What is the source or expression system of G CSF HUMAN, PEG Protein?
Escherichia Coli.

What is the Purity of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of G CSF HUMAN, PEG Protein?
The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

What is the amino acid sequence of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is composed from 175 amino acids.

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

What is the endotoxin level for G CSF HUMAN, PEG Protein?
The endotoxin level is minimal, G CSF HUMAN, PEG 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:

Glucagon Human Recombinant

GLP1, GLP2, GRPP.

Product # :

HOR-237

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Glucagon Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 29 amino acids and having a molecular mass of 3483 Dalton. The Glucagon is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Each mg of recombinant Glucagon was formulated with 100mg of lactose.

Purity

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

Biological Activity

The activity is determind by comparing, under certain conditions, the hyperglycemic effect it produces with that produced by the international standard or by reference preparation calibrated in IU and is found to be 1 IU/mg.

More Info

Introduction
Glucagon is an important hormone involved in carbohydrate metabolism. The hormone is synthesized and secreted from alpha cells (a-cells) of the islets of Langerhans, which are located in the endocrine portion of the pancreas. Glucagon is released when the glucose level in the blood is low (hypoglycemia), causing the liver to convert stored glycogen into glucose and release it into the bloodstream. The action of glucagon is thus opposite to that of insulin, which instructs the body's cells to take in glucose from the blood in times of satiation.
Glucagon is beneficial for the culture of some cell types. It has been used in some biochemical regulation studies of glycogenolysis in hepatocytes. It has been also been found to induce DNA replication in primary cultures of adult rat hepatocytes when used in combinations with EGF and Insulin. Glucagon increases the blood glucose concentration by promoting rapid breakdown of liver glycogen, and also acts to relax smooth muscle such as the gastrointestinal tract.
Synonyms
GLP1, GLP2, GRPP.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Glucagon although stable at room temperature for 3 weeks, should be stored at 40C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Solubility
It is recommended to reconstitute the lyophilized Glucagon sterile 18MΩ-cm H2O not less than 100 µg/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 His-Ser-Gln-Gly-Thr.
Background
What is the molecular weight/Mw of GLUCAGON HUMAN Protein?
GLUCAGON HUMAN Protein has a total Mw of 3.48kDa.

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

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

What is the Biological Activity of GLUCAGON HUMAN Protein?
The activity is determind by comparing, under certain conditions, the hyperglycemic effect it produces with that produced by the international standard or by reference preparation calibrated in IU and is found to be 1 IU/mg.

What is the amino acid sequence of GLUCAGON HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be His-Ser-Gln-Gly-Thr.

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

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

Stromal Cell-Derived Factor-1 gamma Human Recombinant (CXCL12)

Stromal cell-derived factor 1, SDF-1, hSDF-1, C-X-C motif chemokine 12, Intercrine reduced in hepatomas, IRH, hIRH, Pre-B cell growth-stimulating factor, PBSF, CXCL12, SDF1, hSDF-1gamma, SDF-1g, TLSF, TPAR1, SCYB12.

Product # :

CHM-020

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

SDF-1 gamma Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 99 amino acids and having a molecular mass of 11.6kDa.The SDF-1g is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SDF-1g protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biological activity determined by a chemotaxis bioassay using PHA and rHuIL-2 activated human peripheral blood T-lymphocytes is in a concentration range of 30-100 ng/ml.

More Info

Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1a/CXCL12a and SDF-1b/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.
Synonyms
Stromal cell-derived factor 1, SDF-1, hSDF-1, C-X-C motif chemokine 12, Intercrine reduced in hepatomas, IRH, hIRH, Pre-B cell growth-stimulating factor, PBSF, CXCL12, SDF1, hSDF-1gamma, SDF-1g, TLSF, TPAR1, SCYB12.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SDF-1g although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SDF-1 gamma 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 SDF-1g in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKG RREEKVGKKE KIGKKKRQKK RKAAQKRKN.
Background
What is the molecular weight/Mw of CXCL12 HUMAN GAMMA Protein?
CXCL12 HUMAN GAMMA Protein has a total Mw of 11.6kDa.

What is the source or expression system of CXCL12 HUMAN GAMMA Protein?
Escherichia Coli.

What is the Purity of CXCL12 HUMAN GAMMA Protein?
CXCL12 HUMAN GAMMA Protein is > 96% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL12 HUMAN GAMMA Protein?
The biological activity determined by a chemotaxis bioassay using PHA and rHuIL-2 activated human peripheral blood T-lymphocytes is in a concentration range of 30-100 ng/ml.

What is the amino acid sequence of CXCL12 HUMAN GAMMA Protein?
GKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKG RREEKVGKKE KIGKKKRQKK RKAAQKRKN.

What applications can CXCL12 HUMAN GAMMA Protein be used in?
CXCL12 HUMAN GAMMA Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL12 HUMAN GAMMA Protein?
The endotoxin level is minimal, CXCL12 HUMAN GAMMA Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL12 HUMAN GAMMA 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 CXCL12 HUMAN GAMMA?
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.

Country/region

Search results

More Info

Description

Formulation

Purity

Citations

More Info

More Info

Description

Formulation

Purity

Citations

More Info

More Info

Description

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

SDS-PAGE

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description