Search: 1000 results found for "Glucagon"

Description:

Glucokinase E.coli Recombinant, BioActive

Glucokinase, ECK2384, JW2385.

Product # :

PKA-121

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Description

GLK E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (1-321) and having a molecular mass of 37.1kDa.GLK is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GLK protein solution (1mg/ml) contains 0.15M NaCl, 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 70unit/mg obtained by measuring the increase of NADPH in absorbance at 340 nm resulting from the reduction of NADP. One unit will oxidize 1.0 umole of Glucose to D-glucose 6-phosphate per minute in the presence of Beta-NADP at pH 9.0 at 37C.

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Introduction
Glucokinase or GLK, is a protein, part of the bacterial glucokinase superfamily. In the bacteria E. coli, glucose can be transported to the inner cell through a system called PTS as glucose 6-phosphate, therefore, GLK is less crucial to the bacteria.
Synonyms
Glucokinase, ECK2384, JW2385.
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 MGSMTKYALV GDVGGTNARL ALCDIASGEI SQAKTYSGLD YPSLEAVIRV YLEEHKVEVK DGCIAIACPI TGDWVAMTNH TWAFSIAEMK KNLGFSHLEI INDFTAVSMA IPMLKKEHLI QFGGAEPVEG KPIAVYGAGT GLGVAHLVHV DKRWVSLPGE GGHVDFAPNS EEEAIILEIL RAEIGHVSAE RVLSGPGLVN LYRAIVKADN RLPENLKPKD ITERALADSC TDCRRALSLF CVIMGRFGGN LALNLGTFGG VFIAGGIVPR FLEFFKASGF RAAFEDKGRF KEYVHDIPVY LIVHDNPGLL GSGAHLRQTL GHIL

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:

PNC-27

Product # :

HOR-038

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Description

PNC-27 Synthetic is a single, non-glycosylated polypeptide chain containing 32 amino acids, having a molecular mass of 4031.72 Dalton and a Molecular formula of C188H293N53O44S.

Formulation

The protein was lyophilized with no additives.

Purity

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

HPLC, MS

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PNC-27 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PNC-27 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 PNC-27 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-Pro-Pro-Leu-Ser-Gln-Glu-Thr-Phe-Ser-Asp-Leu-Trp-Lys-Leu-Leu-Lys-Lys-Trp-Lys-Met-Arg-Arg-Asn-Gln-Phe-Trp-Val-Lys-Val-Gln-Arg-Gly-OH
Background
PNC-27, a promising anticancer peptide, has gained attention due to its selective cytotoxicity against cancer cells without harming normal cells. This paper aims to elucidate the biochemical characteristics of PNC-27 and explore its potential therapeutic applications in the field of oncology.
PNC-27, a novel anticancer peptide, holds great promise in the treatment of cancer due to its unique mechanism of action and selective cytotoxicity towards cancer cells (Goldberg et al., 2010). This paper seeks to delve into the biochemical attributes of PNC-27 and its therapeutic potential in cancer treatment.
Derived from the p53 tumor-suppressor protein, PNC-27 exhibits a unique binding affinity for the MDM-2 protein found in the membranes of cancer cells. This binding triggers membrane pore formation, leading to cell lysis and death, leaving normal cells unaffected (Goldberg et al., 2010).
Preclinical studies have highlighted the potential of PNC-27 in treating various types of cancers. Its ability to induce cell death in cancer cells without harming normal cells presents a promising direction for cancer therapeutics. For instance, studies have shown PNC-27 to be effective against lung and breast cancers (Hoshino et al., 2011; Sarafraz-Yazdi et al., 2010).
The promising potential of PNC-27 warrants further exploration in clinical trials to evaluate its efficacy and safety in humans. Furthermore, investigation into its synergistic effects with other cancer treatments could provide a more holistic approach to cancer therapeutics. In conclusion, PNC-27 presents an exciting avenue for cancer research, offering a novel and targeted approach to cancer treatment.

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:

Advanced Glycosylation End Product-Specific Receptor Human Recombinant

Advanced glycosylation end product-specific receptor, Receptor for advanced glycosylation end products, AGER, SRAGE, RAGE, MGC22357.

Product # :

PRO-600

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Description

sRAGE Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 339 amino acids and having a molecular mass of 36.5 kDa. The Human sRAGE is fused to a 14 a.a. His tag at N-Terminus.The Human sRAGE is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The sterile filtered (0.4 µm) concentrated (0.5mg/ml) protein solution was lyophilized with 30mM acetate buffer pH-4.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
sRAGE is a member of the immunoglobulin superfamily of cell surface molecules. sRAGE is a receptor for various molecules, including the amyloidogenic form of serum amyloid A, amyloid-beta protein, members of the S100/calgranulin superfamily and advanced glycation end products. sRAGE lies within the major histocompatibility complex (MHC) class III region on chromosome 6. Alternative splicing results in two transcript variants encoding different isoforms. sRAGE mediates interactions of nonenzymatic glycosylated proteins which accumulate in vascular tissue during aging & at an increasing rate in diabetes. sRAGE is a receptor for amyloid beta peptide.
Synonyms
Advanced glycosylation end product-specific receptor, Receptor for advanced glycosylation end products, AGER, SRAGE, RAGE, MGC22357.
Physical Appearance
Sterile 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.
Solubility
Add 0.1M Acetate buffer pH4 to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.
Amino Acid Sequence
MRGSHHHHHH GMASAQNITA RIGEPLVLKC KGAPKKPPQR LEWKLNTGRT EAWKVLSPQG GGPWDSVARV LPNGSLFLPAV GIQDEGIFRCQ AMNRNGKETKS NYRVRVYQIP GKPEIVDSASE LTAGVPNKVG TCVSEGSYPA GTLSWHLDGKPL VPNEKGVSVK EQTRRHPETG LFTLQSELMV TPARGGDPRP TFSCSFSPGL PRHRALRTAP IQPRVWEPVPL EEVQLVVEPE GGAVAPGGTV TLTCEVPAQP SPQIHWMKDGVP LPLPPSPVLI LPEIGPQDQG TYSCVATHSS HGPQESRAVS ISIIEPGEEG PTAGEGFDKV REAEDSPQHM

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:

Chromogranin A Human Recombinant, HEK

CHGA, CGA, Chromogranin-A, Vasostatin I, SP-I, Pituitary secretory protein I.

Product # :

PRO-2664

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Description

CHGA Human Recombinant is a single, glycosylated polypeptide chain containing 445 amino acids (19-457a.a) and having a molecular mass of 49.7kDa (calculated). CHGA is fused to a 6 a.a His tag at C-terminal.

Source

HEK293 cells.

Formulation

CHGA filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS, pH 7.0.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Chromogranin A is a 439 amino acid protein which is encoded on chromosome 14 and is present in neuroendocrine cells throughout the body, including the neuroendocrine cells of the large and small intestine, adrenal medulla and pancreatic islets. It is an excellent marker for carcinoid tumors, phenochromocytomas, paragangliomas, and other neuroendocrine tumors.
Coexpression of chromogranin A and neuron specific enolase (NSE) is common in neuroendocrine neoplasms.
Synonyms
CHGA, CGA, Chromogranin-A, Vasostatin I, SP-I, Pituitary secretory protein I.
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.
Amino Acid Sequence
LPVNSPMNKG DTEVMKCIVE VISDTLSKPS PMPVSQECFE TLRGDERILS ILRHQNLLKE LQDLALQGAK ERAHQQKKHS GFEDELSEVL ENQSSQAELK EAVEEPSSKD VMEKREDSKE AEKSGEATDG ARPQALPEPM QESKAEGNNQ APGEEEEEEE EATNTHPPAS LPSQKYPGPQ AEGDSEGLSQ GLVDREKGLS AEPGWQAKRE EEEEEEEEAE AGEEAVPEEE GPTVVLNPHP SLGYKEIRKG ESRSEALAVD GAGKPGAEEA QDPEGKGEQE HSQQKEEEEE MAVVPQGLFR GGKSGELEQE EERLSKEWED SKRWSKMDQL AKELTAEKRL EGQEEEEDNR DSSMKLSFRA RAYGFRGPGP QLRRGWRPSS REDSLEAGLP LQVRGYPEEK KEEEGSANRR PEDQELESLS AIEAELEKVA HQLQALRRGH 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:

within BCGN Homolog Human Recombinant

PYM, Partner of Y14 and mago, MGC13064, WIBG, BCGN Homolog, Protein wibg homolog.

Product # :

PRO-864

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Description

WIBG Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-204 a.a.) and having a molecular mass of 23.7 kDa. The WIBG is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

WIBG Human solution containing 20mM Tris pH-8, 0.1M NaCl & 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
WIBG is a cooperateing partner of Mago-Y14. The Mago-Y14 heterodimer is a key protein of the EJC(exon junction complex) that is deposited on mRNAs as a consequence of splicing and influences postsplicing mRNA metabolism. WIBG is a cytoplasmic RNA-binding protein that is excluded from the nucleus by Crm1. WIBG relates directly with Mago-Y14 by means of its N-terminal domain.
Synonyms
PYM, Partner of Y14 and mago, MGC13064, WIBG, BCGN Homolog, Protein wibg homolog.
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
MEAAGSPAAT ETGKYIASTQ RPDGTWRKQR RVKEGYVPQE EVPVYENKYV KFFKSKPELP PGLSPEATAP VTPSRPEGGE PGLSKTAKRN LKRKEKRRQQ QEKGEAEALS RTLDKVSLEE TAQLPSAPQG SRAAPTAASD QPDSAATTEK AKKIKNLKKK LRQVEELQQR IQAGEVSQPS KEQLEKLARR RALEEELEDL ELGLLEHHHH 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:

Epiregulin Human Recombinant, His Tag

Epiregulin, Proepiregulin, ER, ERP.

Product # :

CYT-859

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Description

EREG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 69 amino acids (63-108 a.a) and having a molecular mass of 7.7kDa. EREG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

EREG protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE

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Introduction
Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.
Synonyms
Epiregulin, Proepiregulin, ER, ERP.
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 MGSVSITKCS SDMNGYCLHG QCIYLVDMSQ NYCRCEVGYT GVRCEHFFL.
Background
What is the molecular weight/Mw of EREG Protein?
EREG Protein has a total Mw of 7.7kDa.

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

What is the Purity of EREG Protein?
EREG Protein is >80% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of EREG Protein?
MGSSHHHHHH SSGLVPRGSH MGSVSITKCS SDMNGYCLHG QCIYLVDMSQ NYCRCEVGYT GVRCEHFFL.

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

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

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Description:

Atosiban

Product # :

HOR-239

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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

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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.

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:

Pegylated Mouse Leptin Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-591

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Description

Leptin Mono-Pegylated Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and an additional Ala at N-terminus. Pegylated Mouse Leptin contains PEG 20 kDa at its N-terminus and having a molecular mass of 35.6 kDa as determined by mass spectrometry. Since its enlarged hydrodymanic volume Pegylated Leptin runs on SDS-PAGE as A 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Pegylated Mouse Leptin half-life in circulation after SC injection was over 20 hours. Mouse Leptin was purified by proprietary chromatographic techniques according to Salomon et al (2006) Protein Expression and Purification 47, 128–136 and then pegylated.

Source

Escherichia Coli.

Formulation

The mouse Leptin was lyophilized from a concentrated (0.65mg/ml) solution containing 0.003mM NaHCO3.

Purity

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

Biological Activity

Pegylated mouse Leptin is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated mouse Leptin in vitro activity is only slightly lower than the non-pegylated antagonist but in vivo it has profound weight reducing effect (as compared to the non-pegylated leptin), resulting mainly from reduced food intake.

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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile 0.4% NaHCO3 adjusted to pH-8.5 not less than 100µg/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:

Calcitonin Acetate Salmon

CT, KC, CGRP, CALC1, CGRP1, CGRP-I, MGC126648, katacalcin, Calcitonin gene-related peptide 1 precursor, Calcitonin gene-related peptide I.

Product # :

HOR-262

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Description

Calcitonin Acetate (Salmon) is a synthetic polypeptide of 32 amino acids in the same linear sequence that is found in calcitonin of salmon origin. The Molecular Formula is C145H240N44O48S2. Calcitonin Molecular Weight: 3431.9 Dalton.

Formulation

The calcitonin peptide 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
Calcitonin (CT) is a peptide hormone produced by the parafollicular cells of the thyroid gland in mammals and by the ultimobranchial gland of birds and fish. Salmon calcitonin (sCT), which is more potent and longer lasting than human CT, has been used widely for the treatment of osteoporosis, paget's disease, hypercalcemic shock and chronic pain in terminal cancer patients. sCT is one of the many bioactive peptides that require C-terminal amidation for full biological activity.
Synonyms
CT, KC, CGRP, CALC1, CGRP1, CGRP-I, MGC126648, katacalcin, Calcitonin gene-related peptide 1 precursor, Calcitonin gene-related peptide I.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Calcitonin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CGRP 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 Calcitonin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Calcitonin Acetate (Salmon) has an amino acid sequence of: Cys-Ser-Asn-Leu-Ser-Thr-Cys-Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn-Thr-Gly-Ser-Gly-Thr-Pro-NH2.

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Description:

Aprotinin

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

Product # :

PRO-285

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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:

Adiponectin Human Recombinant, HEK

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-434

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Description

Acrp30 Human Recombinant produced in HEK cells is a glycosylated polypeptide chain containing 234 amino acids (19-244a.a.) and having a molecular mass of 25.5kDa. Acrp30 is expressed with a FLAG tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

HEK293 (Human Embryonic Kidney cell line).

Formulation

Filtered (0.4µm) and lyophilized from 0.5mg/ml in 50mM phosphate Buffer, 75mM NaCl, pH 7.4.

Purity

Greater than 98% as determined by HPLC and SDS PAGE.

Biological Activity

In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.

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Introduction
Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
For long term, store lyophilized AdipoQ 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. The lyophilized protein remains stable for 24 months when stored at -20°C.
Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product not sterile! Please filter the product by an appropriate sterile filter before using it in cell culture.
Amino Acid Sequence
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.
Background
What is the molecular weight/Mw of adiponectin Protein?
Adiponectin Protein has a total Mw of 25.5kDa.

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

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

What is the Biological Activity of adiponectin Protein?
In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.

What is the amino acid sequence of adiponectin Protein?
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.

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

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

Adiponectin Mouse Recombinant, His Tag

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-537

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Description

The Adiponectin Mouse is created as a recombinant protein with a 21 a.a N-terminal fusion of His Tag. The Adiponectin His-Tagged Fusion Protein, produced in E. coli, is a 27.2kDa protein containing 251 amino acid residues of the Acrp30 Mouse, 18-247 amino acids.

Source

Escherichia Coli.

Formulation

Acrp30 Mouse is a sterile filtered liquid formulation containing (1mg/ml) 20mM Tris-HCl pH-8, 1mM DTT and 10% Glycerol.

Purity

Acrp30 Mouse purity is greater than 90% as determined by SDS-PAGE.

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Introduction
Adiponectin is an adipocyte specific secreted protein that circulates in the plasma. It is induced during adipocyte differentiation and its secretion is stimulated by insulin. Mouse adiponectin shares about 83% amino acid identity with that human. Adiponectin plays a role in various physiological processes such as energy homeostasis and obesity. Adiponectin is reduced in obese humans, and decreased level is associated with insulin resistance and hyperinsulinemia.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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 MEDDVTTTEE LAPALVPPPK GTCAGWMAGI PGHPGHNGTP GRDGRDGTPG EKGEKGDAGL LGPKGETGDV GMTGAEGPRG FPGTPGRKGE PGEAAYVYRS AFSVGLETRV TVPNVPIRFT KIFYNQQNHY DGSTGKFYCN IPGLYYFSYH ITVYMKDVKV SLFKKDKAVL FTYDQYQEKN VDQASGSVLL HLEVGDQVWL QVYGDGDHNG LYADNVNDST FTGFLLYHDT N.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 27.2kDa.

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

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

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

What is the amino acid sequence of ADIPONECTIN Protein?
MGSSHHHHHH SSGLVPRGSH MEDDVTTTEE LAPALVPPPK GTCAGWMAGI PGHPGHNGTP GRDGRDGTPG EKGEKGDAGL LGPKGETGDV GMTGAEGPRG FPGTPGRKGE PGEAAYVYRS AFSVGLETRV TVPNVPIRFT KIFYNQQNHY DGSTGKFYCN IPGLYYFSYH ITVYMKDVKV SLFKKDKAVL FTYDQYQEKN VDQASGSVLL HLEVGDQVWL QVYGDGDHNG LYADNVNDST FTGFLLYHDT N.

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

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

Glutaredoxin-3 Human Recombinant

Glutaredoxin-3, Thioredoxin-like protein 2, PKC-interacting cousin of thioredoxin, PKC-theta-interacting protein, PKCq-interacting protein, GLRX3, PICOT, TXNL2, GRX3, GRX4, GLRX4, TXNL3, FLJ11864, bA500G10.4.

Product # :

ENZ-482

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Description

GLRX3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 355 amino acids (1-335 a.a.) and having a molecular mass of 39.6kDa. GLRX3 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GLRX3 solution containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 1mM DTT.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Glutaredoxin belongs to the thiol-disulfide oxidoreductase family. Glutraredoxins catalyze the reversible reduction of protein-glutathionyl mixed disulfides to free sulfhydryl groups though a monothiol mechanism. Glutaredoxin-3 (GRX3) is an important protein involved in the regulation of signal transduction, for example during immune cell activation and development of cardiac hypertrophy, apparently in response to redox signals. GRX3 interacts with PRKCQ. GRX3 may have a role in the regulation the function of the thioredoxin system. GRX3 is expressed in the heart, spleen, testis and, to a lower extent, in the thymus and peripheral blood leukocytes. GRX3 is weakly expressed in lung, placenta, colon and small intestine.
Synonyms
Glutaredoxin-3, Thioredoxin-like protein 2, PKC-interacting cousin of thioredoxin, PKC-theta-interacting protein, PKCq-interacting protein, GLRX3, PICOT, TXNL2, GRX3, GRX4, GLRX4, TXNL3, FLJ11864, bA500G10.4.
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 MAAGAAEAAV AAVEEVGSAG QFEELLRLKA KSLLVVHFWA PWAPQCAQMN EVMAELAKEL PQVSFVKLEA EGVPEVSEKY EISSVPTFLF FKNSQKIDRL DGAHAPELTK KVQRHASSGS FLPSANEHLK EDLNLRLKKL THAAPCMLFM KGTPQEPRCG FSKQMVEILH KHNIQFSSFD IFSDEEVRQG LKAYSSWPTY PQLYVSGELI GGLDIIKELE ASEELDTICP KAPKLEERLK VLTNKASVML FMKGNKQEAK CGFSKQILEI LNSTGVEYET FDILEDEEVR QGLKAYSNWP TYPQLYVKGE LVGGLDIVKE LKENGELLPI LRGEN.

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:

Betacellulin Human Recombinant

Product # :

CYT-330

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Description

Betacellulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and having a molecular mass of 9 kDa. Betacellulin Human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Betacellulin Human Recombinant was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

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

Biological Activity

The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml. corresponding to a Specific Activity of >20,000,000IU/mg.

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Introduction
Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Betacellulin Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BTC Human 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 BTC Human in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY
Background
Betacellulin Human Recombinant: Illuminating Pathways in Regenerative Medicine
Introduction
In the ever-evolving landscape of regenerative medicine, a promising new chapter unfolds with the arrival of Betacellulin Human Recombinant (BTC). This growth factor holds tremendous potential, offering a glimpse into the future of transformative therapeutic interventions.
BTC: The Architect of Cellular Revitalization
BTC, a member of the EGF family, has long been recognized for its pivotal role in cellular proliferation and differentiation. The emergence of BTC in its recombinant form has sparked excitement, igniting new possibilities for regenerative medicine.
Crafting the Alchemist: Pioneering Methodologies
Through the adept utilization of biotechnological techniques, we successfully synthesized BTC human recombinant. Our meticulous in vitro investigations delved into BTC's capacity to orchestrate intricate cellular processes, paving the way for therapeutic advancements.
Unveiling the Biological Tapestry
Buoyed by encouraging in vitro findings, we embarked on in vivo studies utilizing animal models. This natural setting allowed us to witness BTC human recombinant's impact within a living organism, unraveling the intricate nuances of its regenerative potential.
A Flourish of Results
The journey from laboratory to living system yielded promising results. BTC human recombinant showcased a significant influence on cellular proliferation and differentiation, underscoring its role as a key player in tissue regeneration and regenerative therapies.
Charting a Transformative Future
As the story of BTC human recombinant unfolds, it beckons further exploration through extensive human-centric clinical trials. These trials will serve as a compass, guiding us towards harnessing the full therapeutic potential of BTC, ushering in a new era of healing and regeneration.
What is the molecular weight/Mw of BTC Protein?
BTC Protein has a total Mw of 9kDa.

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

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

What is the Biological Activity of BTC Protein?
The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml. corresponding to a Specific Activity of >20,000,000IU/mg.

What is the amino acid sequence of BTC Protein?
DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY

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

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

Epiregulin Human Recombinant, HEK

EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.

Product # :

CYT-1206

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Description

EREG Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (63-108a.a) containing 289 amino acids and having a molecular mass of 32.6 kDa.EREG is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

EREG protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.

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Introduction
"Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence."
Synonyms
EPR, Epiregulin, Ep, ER, Proepiregulin, EREG.
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
DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH
Background
What is the molecular weight/Mw of EREG Protein?
EREG Protein has a total Mw of 32.6kDa.

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

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

What is the Biological Activity of EREG Protein?
Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 1ug/ml.

What is the amino acid sequence of EREG Protein?
DGSMVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH

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

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

Placental Lactogen Human Recombinant

Chorionic Somatomammotropin Hormone 1, CSH1, Choriomammotropin, Lactogen, CSH2, PL, CSA, CSMT, FLJ75407.

Product # :

CYT-656

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Description

Placental Lactogen Human Recombinant, is a single polypeptide chain containing 199 amino acids and an additional Ala at the N-terminus having a molecular mass of approximately 22.4 kDa. Placental Lactogen Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.

Purity

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

Biological Activity

Placental Lactogen Human is biologically active as evidenced by inducing proliferation of Nb2 cells.

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Introduction
Placental Lactogen is a polypeptide hormone that is produced by the Syncytiotrophoblasts of the Placenta, also known as chorionic somatomammotropin. It has both GH and Prolactin activities on growth, lactation, and luteal steroid production. In women, placental lactogen secretion begins soon after implantation and increases to 1 g or more a day in late pregnancy. Placental lactogen is also an ins. antagonist.
Placental Lactogen Bovine is also capable of activating human and other heterologous GH receptors but not ruminat GH receptors.
Synonyms
Chorionic Somatomammotropin Hormone 1, CSH1, Choriomammotropin, Lactogen, CSH2, PL, CSA, CSMT, FLJ75407.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Placental Lactogen Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Placental Lactogen 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 Placental Lactogen in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.
Amino Acid Sequence
The sequence of the first 6 N-terminal amino acids was determined and was found to be Ala-Val-Gln-Thr-Val-Pro.
Protein content
UV spectroscopy at 280 nm using the absorbency value of 0.73 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the DNAman computer analysis program of protein sequences.

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:

SEMAX

Product # :

HOR-033

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Description

SEMAX Synthetic is a single, non-glycosylated polypeptide chain containing 7 amino acids, having a molecular mass of 813.92 Dalton and a Molecular formula of C37H51N19O1S.

Formulation

The protein was lyophilized with no additives.

Purity

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

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SEMAX although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SEMAX 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 SEMAX 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-Met-Glu-His-Phe-Pro-Gly-Pro-OH.
Background
Semax, also known as ACTH(4-10) Pro-Gly-Pro, is a synthetic peptide that has been the subject of extensive research due to its potential neuroprotective and nootropic effects. This heptapeptide, derived from the adrenocorticotropic hormone (ACTH), has been shown to possess a wide range of biological activities, including enhancing memory, learning, and neurogenesis.
Semax is unique in its ability to cross the blood-brain barrier and exert its effects directly on the central nervous system. It has been shown to stimulate the release of brain-derived neurotrophic factor (BDNF), a protein that plays a crucial role in the survival of neurons and the growth of new neurons and synapses. Studies by Dolotov et al. (2006) have demonstrated that Semax can enhance memory and learning in rats, suggesting potential applications in cognitive enhancement and the treatment of cognitive disorders.
In addition to its nootropic effects, Semax has been shown to possess neuroprotective properties. Research by Stavchansky et al. (2008) found that Semax could protect neurons from oxidative stress and apoptosis, suggesting potential applications in the treatment of neurodegenerative diseases such as Alzheimer's and Parkinson's disease.
Given its nootropic and neuroprotective effects, Semax has been proposed as a potential therapeutic agent for a variety of conditions, including cognitive disorders, stroke, and optic nerve disease. For instance, a study by Myasoedov et al. (2010) found that Semax could improve outcomes in patients with ischemic stroke, indicating its potential as a therapeutic agent in stroke recovery.
While research on Semax 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 Semax in humans. However, the existing body of research suggests that Semax could be a promising tool in the treatment of cognitive disorders 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:

Vasoactive Intestinal Peptide

Product # :

HOR-043

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Description

Vasoactive Intestinal Peptide Synthetic is a single, non-glycosylated polypeptide chain containing 28 amino acids, having a molecular mass of 3325 Dalton and a Molecular formula of C147H238N44O42S .

Formulation

The protein was lyophilized with no additives.

Purity

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

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Vasoactive Intestinal Peptide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Vasoactive Intestinal Peptide 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 Vasoactive Intestinal Peptide 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-Ser-Asp-Ala-Val-Phe-Thr-Asp-Asn-Tyr-Thr-Arg-Leu-Arg-Lys-Gln-Met-Ala-Val-Lys-Lys-Tyr-Leu-Asn-Ser-Ile-Leu-Asn-NH2.
Background
Vasoactive Intestinal Peptide (VIP), a prominent member of the glucagon-secretin peptide superfamily, plays a multifaceted role as a neuropeptide and neurotransmitter. This research paper aims to provide an extensive analysis of VIP, exploring its biochemical properties, diverse physiological functions, and potential therapeutic applications in various disease conditions.
Vasoactive Intestinal Peptide (VIP), originally identified for its potent vasodilatory properties in the gastrointestinal system, has since been recognized for its wide-ranging physiological effects throughout the body. As a neuropeptide and neurotransmitter.
VIP, a 28-amino acid peptide, exhibits a diverse range of biological activities due to its interactions with multiple G protein-coupled receptors (GPCRs) from the VIP/PACAP receptor family (Harmar et al., 2012). These receptors are expressed in various tissues and cells, enabling VIP to exert its pleiotropic effects.
VIP is involved in the regulation of numerous physiological processes. It functions as a potent vasodilator, modulates smooth muscle activity in the gastrointestinal tract, and participates in neurotransmission in the central and peripheral nervous systems (Lelievre et al., 2008). Additionally, VIP has immunomodulatory properties, influencing immune cell functions and inflammatory responses (Delgado et al., 2004).
VIP serves as a neurotransmitter in the central nervous system, where it contributes to various neuronal functions, including learning, memory, and sensory perception (Deng et al., 2015). Moreover, VIP has demonstrated neuroprotective effects in neurodegenerative disorders, making it a potential therapeutic target for neuroprotection and neuroregeneration (Delgado et al., 2002).
VIP's diverse physiological functions offer potential therapeutic applications in various disease contexts. Research has explored its potential in the treatment of inflammatory diseases, neurodegenerative disorders, and gastrointestinal disorders (Delgado et al., 2013). Furthermore, VIP-based therapies are being investigated for their neuroprotective potential in brain injuries and stroke.
As the research on VIP continues to progress, further investigation is warranted to uncover the precise mechanisms of action and potential clinical applications in medicine. VIP stands as a remarkable example of a neuropeptide with extensive physiological roles and therapeutic potential in various disease conditions.
What is the molecular weight/Mw of VASOACTIVE INTESTINAL PEPTIDE Protein?
VASOACTIVE INTESTINAL PEPTIDE Protein has a total Mw of 3.32kDa.

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

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

What is the amino acid sequence of VASOACTIVE INTESTINAL PEPTIDE Protein?
H-His-Ser-Asp-Ala-Val-Phe-Thr-Asp-Asn-Tyr-Thr-Arg-Leu-Arg-Lys-Gln-Met-Ala-Val-Lys-Lys-Tyr-Leu-Asn-Ser-Ile-Leu-Asn-NH2.

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

What is the endotoxin level for VASOACTIVE INTESTINAL PEPTIDE Protein?
The endotoxin level is minimal, VASOACTIVE INTESTINAL PEPTIDE 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:

Thyrostimulin Beta Human Recombinant

Glycoprotein hormone beta-5, ZLUT1, GPHB5, GPB5.

Product # :

HOR-257

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Description

GPHB5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 120 amino acids and having a total molecular mass of 13.34 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

The GPHB5 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.

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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
Glycoprotein hormone beta-5, ZLUT1, GPHB5, GPB5.
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 GPHB5 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 GMASASSGNL RTFVGCAVRE FTFLAKKPGC RGLRITTDAC WGRCETWEKP ILEPPYIEAH HRVCTYNETK QVTVKLPNCA PGVDPFYTYP VAIRCDCGAC STATTECETI.

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

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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.

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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:

Inhibin Alpha Human Recombinant

Product # :

HOR-303

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Description

Inhibin-Alpha Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 264 amino acids comprising of both A and B chains, having a molecular mass of 33.5 kDa.The Inhibin-Alpha is fused with an amino-terminal hexahistidine tag. The Inhibin-Alpha is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

Inhibin-A alpha chain is supplied in 20mM Tris and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE analysis.

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Introduction
Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.
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.
Amino Acid Sequence
Alpha chain:
STPLMSWPWSPSALRLLQRPPEEPAAHANCHRVALNISFQELGWERWIVYPPSFIFHYCHGGCGLHIP PNLSLPVPGAPPTPAQPYSLLPGAQPCCAALPGTMRPLHVRTTSDGGYSFKYETVPNLLTQHCACI.

Beta Chain:
GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMR
GHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.

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:

Beta-Glucocerebrosidase Human Recombinant

Glucosidase, Beta, Acid, D-Glucosyl-N-Acylsphingosine Glucohydrolase, Beta-Glucocerebrosidase, Acid Beta-Glucosidase, Glucosylceramidase, Alglucerase, EC 3.2.1.45, Beta-GC, GLUC, Glucosidase, Beta; Acid (Includes Glucosylceramidase), Glucosylceramidase-Like Protein, Lysosomal Glucocerebrosidase, GBA1, GCB, GC, Glucosylceramidase.

Product # :

ENZ-908

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GBA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 503 amino acids (40-536a.a.) and having a molecular mass of 56.4kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). GBA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

GBA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
Beta-Glucocerebrosidase, also known as GBA is amember of the glycosyl hydrolase 30 family. GBA is a lysosomal enzyme which requires a signal peptide for transport across the membrane of the rough endoplasmic reticulum as well as glycosylation for transport into lysosomes. Furthermore, Gaucher disease is caused by a deficiency in the activity of the enzyme glucocerebrosidase.
Synonyms
Glucosidase, Beta, Acid, D-Glucosyl-N-Acylsphingosine Glucohydrolase, Beta-Glucocerebrosidase, Acid Beta-Glucosidase, Glucosylceramidase, Alglucerase, EC 3.2.1.45, Beta-GC, GLUC, Glucosidase, Beta; Acid (Includes Glucosylceramidase), Glucosylceramidase-Like Protein, Lysosomal Glucocerebrosidase, GBA1, GCB, GC, Glucosylceramidase.
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
ARPCIPKSFG YSSVVCVCNA TYCDSFDPPT FPALGTFSRY ESTRSGRRME LSMGPIQANH TGTGLLLTLQ PEQKFQKVKG FGGAMTDAAA LNILALSPPA QNLLLKSYFS EEGIGYNIIR VPMASCDFSI RTYTYADTPD DFQLHNFSLP EEDTKLKIPL IHRALQLAQR PVSLLASPWT SPTWLKTNGA VNGKGSLKGQ PGDIYHQTWA RYFVKFLDAY AEHKLQFWAV TAENEPSAGL LSGYPFQCLG FTPEHQRDFI ARDLGPTLAN STHHNVRLLM LDDQRLLLPH WAKVVLTDPE AAKYVHGIAV HWYLDFLAPA KATLGETHRL FPNTMLFASE ACVGSKFWEQ SVRLGSWDRG MQYSHSIITN LLYHVVGWTD WNLALNPEGG PNWVRNFVDS PIIVDITKDT FYKQPMFYHL GHFSKFIPEG SQRVGLVASQ KNDLDAVALM HPDGSAVVVV LNRSSKDVPL TIKDPAVGFL ETISPGYSIH TYLWRRQHHH HHH.

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:

Leptin Super Antagonist Human Recombinant

Product # :

CYT-1238

Price :

Quantity :

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Shipped at Room temp

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Description

Super Leptin Antagonist Human Recombinant is a single polypeptide chain containing 146 amino acids. Super Human Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A super human leptin antagonist that was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

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

Purity

Greater than 98.0% as determined by:

(a) Gel filtration analysis.

(b) Analysis by SDS-PAGE.

Biological Activity

ProSpec’s super human leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin.

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Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized Super Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of super human leptin antagonist at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization super human leptin antagonist can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Super Leptin Antagonist in sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
Background
Leptin is a hormone which takes part in regulating body weight, metabolism and reproductive function. Leptin is a~16 kDa protein which is encoded by the obese gene. leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.

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:

Chromogranin-A Human Recombinant

CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.

Product # :

PRO-692

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Recombinant Human CHGA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 114 amino acids (19-131 a.a) and having a molecular mass of 12.8 kDa. Chromgranin-A is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CHGA protein contains 20mM Tris-HCl buffer pH-8, and 10% glycerol.

Purity

Greater than 95.0% as determined by analysis by SDS-PAGE.

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Introduction
Chromgranin-A is part of the neuroendocrine secretory protein family. CHGA is located in secretory vesicles of neurons and endocrine cells. Chromgranin-A is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Other peptides, including chromostatin, beta-granin, WE-14 and GE-25, are also derived from the full-length protein. Chromgranin-A has numerous biological activities on some tissues and organs and exerts a large spectrum of homeostatic actions, including antifungal and antimicrobial effect, modulation of cell adhesion, and inhibition of parathyroid hormone secretion.
Synonyms
CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.
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
MLPVNSPMNK GDTEVMKCIV EVISDTLSKP SPMPVSQECF ETLRGDERIL SILRHQNLLK ELQDLALQGA KERAHQQKKH SGFEDELSEV LENQSSQAEL KEAVEEPSSK DVME.

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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