Search: 1000 results found for "Chromogranin"

Description:

Myostatin Propeptide Human Recombinant

GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

Product # :

CYT-448

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Shipped at Room temp

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Description

Recombinant Human Myostatin Propeptide is a 27.8kDa protein containing 244 amino acid residues of the human Myostatin Propeptide.

Source

Escherichia Coli.

Formulation

Lyophilized with no additives.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The protein has full biological activity when compared to a standard. The activity is determined by its ability to inhibit 50ng/ml of Myostatin on MPC-11 cells and is typically 0.13-0.2 μg/ml.

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Introduction
Myostatin (GDF-8), a member of the TGFbeta superfamily, is a potent and specific negative regulator of skeletal muscle mass. In serum, myostatin circulates as part of a latent complex containing myostatin propeptide and/or follistatin-related gene. The myostatin propeptide is known to bind and inhibit myostatin in vitro. This interaction is relevant in vivo, with a majority (>70%) of myostatin in serum bound to its propeptide. The myostatin propeptide is negative regulator of myostatin in vivo.
Synonyms
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
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
It is recommended to reconstitute the lyophilized Myostatin Propeptide in sterile 20mM HCl at 0.1mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MNENSEQKE NVEKEGLCNA CTWRQNTKSS RIEAIKIQIL SKLRLETAPN ISKDVIRQLL PKAPPLRELI DQYDVQRDDS SDGSLEDDDY HATTETIITM PTESDFLMQV DGKPKCCFFK FSSKIQYNKV VKAQLWIYLR PVETPTTVFV QILRLIKPMK DGTRYTGIRS LKLDMNPGTG IWQSIDVKTV LQNWLKQPES NLGIEIKALD ENGHDLAVTF PGPGEDGLNP FLEVKVTDTP KRSRR.

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:

Serglycin Human Recombinant

Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.

Product # :

PRO-965

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Description

SRGN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (28-158) and having a molecular mass of 17.4 kDa (Molecular weight on SDS-PAGE will appear higher).SRGN is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The SRGN solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.15M NaCl and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
SRGN is identified as a hematopoietic cell granule proteoglycan. Proteoglycans stored in the secretory granules of various hematopoietic cells also hold a protease-resistant peptide core, and is vital for neutralizing hydrolytic enzymes. SRGN is related to the macromolecular complex of granzymes and perforin that acts as a intermediary of granule-mediated apoptosis.
Synonyms
Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.
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 MGSHMYPTRR ARYQWVRCNP DSNSANCLEE KGPMFELLPG ESNKIPRLRT DLFPKTRIQD LNRIFPLSED YSGSGFGSGS GSGSGSGSGF LTEMEQDYQL VDESDAFHDN LRSLDRNLPS DSQDLGQHGL EEDFML.

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:

O-Sialoglycoprotein Endopeptidase Human Recombinant

O-Sialoglycoprotein Endopeptidase, T(6)A37 Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, TRNA Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, N6-L-Threonylcarbamoyladenine Synthase, T(6)A Synthase, HOSGEP, GCPL1, Probable TRNA Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, Probable TRNA N6-Adenosine Threonylcarbamoyltransferase , Probable O-Sialoglycoprotein Endopeptidase, EC 3.4.24.57, EC 2.3.1.234, FLJ20411, OSGEP1, PRSMG1, KAE1, Probable tRNA N6-adenosine threonylcarbamoyltransferase.

Product # :

ENZ-821

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Description

OSGEP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (1-335 a.a) and having a molecular mass of 38.8kDa. OSGEP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

OSGEP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
O-Sialoglycoprotein Endopeptidase, also known as OSGEP is a member of the KAE1 / TsaD family. OSGEP is essential for the formation of threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs which read codons beginning with adenine. OSGEP take a direct catalytic part in the above reaction, however other proteins of the complex are required to fulfill this activity.
Synonyms
O-Sialoglycoprotein Endopeptidase, T(6)A37 Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, TRNA Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, N6-L-Threonylcarbamoyladenine Synthase, T(6)A Synthase, HOSGEP, GCPL1, Probable TRNA Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, Probable TRNA N6-Adenosine Threonylcarbamoyltransferase , Probable O-Sialoglycoprotein Endopeptidase, EC 3.4.24.57, EC 2.3.1.234, FLJ20411, OSGEP1, PRSMG1, KAE1, Probable tRNA N6-adenosine threonylcarbamoyltransferase.
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 MGSMPAVLGF EGSANKIGVG VVRDGKVLAN PRRTYVTPPG TGFLPGDTAR HHRAVILDLL QEALTESGLT SQDIDCIAYT KGPGMGAPLV SVAVVARTVA QLWNKPLVGV NHCIGHIEMG RLITGATSPT VLYVSGGNTQ VIAYSEHRYR IFGETIDIAV GNCLDRFARV LKISNDPSPG YNIEQMAKRG KKLVELPYTV KGMDVSFSGI LSFIEDVAHR MLATGECTPE DLCFSLQETV FAMLVEITER AMAHCGSQEA LIVGGVGCNV RLQEMMATMC QERGARLFAT DERFCIDNGA MIAQAGWEMF RAGHRTPLSD SGVTQRYRTD EVEVTWRD.

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:

Luteinizing Hormone Porcine

Product # :

HOR-310

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Description

Porcine Luteinizing Hormone is a glycosylated, heterodimer polypeptide chain which stimulates maturation of follicle, induces ovulation, accelerates formation of corpus luteum and secretion of pregnanolone. Porcine Luteinizing Hormone delays ovulation and ovarian cyst.

Source

Porcine.

Formulation

The LH was lyophilized with no additives.

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Porcine LH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LH 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 Porcine LH in sterile 18M-cm H2O at 100IU/4ml, which can then be further diluted to other aqueous solutions.
Background
What is the source or expression system of LUTEINIZING HORMONE PORCINE Protein?
Porcine.

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

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

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

Who supplies LUTEINIZING HORMONE PORCINE 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 LUTEINIZING HORMONE PORCINE?
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:

Procalcitonin Rhesus Recombinant

Calcitonin.

Product # :

HOR-016

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Description

Procalcitonin Rhesus Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Ala26-Asn140) containing 125 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 14kDa.

Source

Escherichia Coli.

Formulation

Procalcitonin was filtered (0.4µm) and lyophilized from 0.5mg/ml solution in 20mM Tris buffer and 50mM NaCl, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.
Synonyms
Calcitonin.
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 0.5 mg/ml and let the lyophilized pellet dissolve completely. Procalcitonin is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHASAPFRSALESS PDPATLSEEE ARLLLAALVQ DYVQMKASEL EQEQETEGSS LDSPRSKRCG NLSTCMLGTY TQDFNKFHTF PQTAIGVGAP GKKRDMSSDL ERNRRRYVSM PQDAN.
Background
What is the molecular weight/Mw of PROCALCITONIN RHESUS Protein?
PROCALCITONIN RHESUS Protein has a total Mw of 14kDa.

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

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

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

What is the amino acid sequence of PROCALCITONIN RHESUS Protein?
MKHHHHHHASAPFRSALESS PDPATLSEEE ARLLLAALVQ DYVQMKASEL EQEQETEGSS LDSPRSKRCG NLSTCMLGTY TQDFNKFHTF PQTAIGVGAP GKKRDMSSDL ERNRRRYVSM PQDAN.

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

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

Who supplies recombinant PROCALCITONIN RHESUS 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 PROCALCITONIN RHESUS?
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:

Nafarelin Acetate

Product # :

HOR-248

Price :

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Shipped at Room temp

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Description

Nafarelin is a decapeptide containing 9 amino acids Glu-His-Trp-Ser-Ala-Leu-Arg-Pro.Nafarelin is purified by proprietary chromatographic techniques.

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.

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Introduction
Nafarelin acetate is a synthetic analog of the naturally occurring gonadotropin-releasing hormone (GnRH). Nafarelin stimulates the release of the pituitary gonadotropins, LH and FSH, resulting in a temporary increase of ovarian steroidogenesis.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Nafarelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NAF 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 Nafarelin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Glu-His-Trp-Ser-Ala-Leu-Arg-Pro.
Background
What is the Purity of NAFARELIN Protein?
NAFARELIN Protein is >98% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of NAFARELIN Protein?
Glu-His-Trp-Ser-Ala-Leu-Arg-Pro.

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

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

Who supplies NAFARELIN 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 NAFARELIN?
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:

Secretagogin Rat Recombinant

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

Product # :

PRO-657

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Secretagogin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 286 amino acids and having a molecular mass of 33.3 kDa. The Rat SCGN is fused to a 10 a.a. His tag at N-Terminus.The protein’s amino acids sequence is identical to UniProtKB/Swiss-Prot entry Q6R556.The Rat SCGN is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The sterile filtered concentrated protein solution was lyophilized with 20mM Tris & 50mM NaCl pH-7.5.

Purity

Greater than 95% as determined by SDS-PAGE.

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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, Secretagogin.
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 deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.
Amino Acid Sequence
MKHHHHHHAS MDNAHRQTQA HLDAACFWQI WQRFDKDEKG YIKETELDAF FDDLLAKFGI EDTLMEENVQ KMKEQLMVGH DISKEGRILM KELASMFLSE DENFLLFFRL ETPLDNSVEF MQIWRKYDAD SSGFISAAEL SNFLRDLFLH HKKVISEAEL EEYTSTMMKI FDRNKDGRLD LNDLARILAL QENFLLQFKM DASSTEERKR DFEKIFAHYD VSKTGALEGP EVDGFVKDMM ELVQPSISGV DLDKFREILL RHCDVNKDGK IQKSELALCLGLKINP.

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:

Cathepsin-D Human Recombinant

Cathepsin D, EC 3.4.23.5, CTSD, CPSD, CLN10, MGC2311.

Product # :

ENZ-378

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Description

CTSD produced in HEK293 cells is a single, glycosylated polypeptide chain containing 398 amino acids (21-412 a.a.) and having a molecular mass of 43.4kDa. CTSD is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

HEK293 Cells

Formulation

CTSD at 1mg/ml in 50mM MES, pH5.5, 100mM NaCl and 20% Glycerol.

Purity

Greater than 95% as determined by SDS-PAGE

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Introduction
Cathepsin D is synthesized as a 54kDa precursor, which is proteolytically processed to an intermediate 48kDa single chain, which matures into more stable 34kDa and 14kDa two chain form. It is an estrogen-regulated lysosomal protease that has been suggested to facilitate cancer cell migration and invasion by digesting the basement membrane, extracellular matrix, and xonnective tissue. Because of its mitogenic and proteolytic activities, it has been implicated as a prognostic marker in many tumor types. Cathepsin D is expressed in epithelial cells as well as in macrophages.
Synonyms
Cathepsin D, EC 3.4.23.5, CTSD, CPSD, CLN10, MGC2311.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.
Amino Acid Sequence
LVRIPLHKFT SIRRTMSEVG GSVEDLIAKG PVSKYSQAVP AVTEGPIPEV LKNYMDAQYY GEIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KLLDIACWIH HKYNSDKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC QSASSASALG GVKVERQVFG EATKQPGITF IAAKFDGILG MAYPRISVNN VLPVFDNLMQ QKLVDQNIFS FYLSRDPDAQ PGGELMLGGT DSKYYKGSLS YLNVTRKAYW QVHLDQVEVA SGLTLCKEGC EAIVDTGTSL MVGPVDEVRE LQKAIGAVPL IQGEYMIPCE KVSTLPAITL KLGGKGYKLS PEDYTLKVSQ AGKTLCLSGF MGMDIPPPSG PLWILGDVFI GRYYTVFDRD NNRVGFAEAA RLHHHHHH
Enzymatic Activity
> 20 pmol/min/ug, defined as the amount of enzyme which cleaves 1pmol of Mca-PLGLDpa-AR-NH2/min at pH-3.5 at 25C.

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:

Peptidase Inhibitor 16 Human Recombinant

Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.

Product # :

ENZ-113

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

The Peptidase Inhibitor 16 Human Recombinant is produced in HEK293 cells and fused with a C-terminal Flag Tag (11 amino acids). The PI16 Flag Tagged Fusion Protein is 45.7kDa protein containing a total of 426 amino acid residues and purified by proprietary chromatographic techniques.

Source

HEK293 (Human Embryonic Kidney cell line).

Formulation

PI16 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Peptidase Inhibitor 16 (PI16) which a member of the CRISP family, is a putative serine protease inhibitor. PI16 interacts with PSP94/MSMB. PI16 is expressed in the prostate, testis, ovary and intestine. It also concentrates in prostate cancer patient's sera. PI16 may serve as a marker following prostatectomy for prostate cancer.
Synonyms
Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized PI16 Human recombinant 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 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
LTDEEKRLMV ELHNLYRAQV SPPASDMLHM RWDEELAAFA KAYARQCVWG HNKERGRRGE NLFAITDEGM DVPLAMEEWH HEREHYNLSA ATCSPGQMCG HYTQVVWAKT ERIGCGSHFC EKLQGVEETN IELLVCNYEP PGNVKGKRPY QEGTPCSQCP SGYHCKNSLC EPIGSPEDAQ DLPYLVTEAP SFRATEASDS RKMGTPSSLA TGIPAFLVTE VSGSLATKAL PAVETQAPTS LATKDPPSMA TEAPPCVTTE VPSILAAHSL PSLDEEPVTF PKSTHVPIPK SADKVTDKTK VPSRSPENSL DPKMSLTGAR ELLPHAQEEA EAEAELPPSS EVLASVFPAQ DKPGELQATL DHTGHTSSKS LPNFPNTSAT ANATGGRALA LQSSLPGAEG PDKPSVVSGL NSGPGAAADYKDDDDK.

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:

Prolactin Receptor Antagonist Human Recombinant

Mammotropin, Luteotropic hormone, Luteotropin, PRL.

Product # :

CYT-1254

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Prolactin Human Receptor Antagonist del 1-9, G129R mutant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids + an additional Ala at n-terminal and having a molecular mass of ~ 22 kDa. The Human Prolactin Receptor Antagonist is purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The protein was lyophilized from a concentrated (1-2mg/ml) solution with 0.02% -0.03% NaHCO3.

Purity

Greater than 97.0% as determined by:

(a) Analysis by Gel Filtration.

(b) Analysis by SDS-PAGE.

Biological Activity

fully biologically active as evidenced by inhibiting PRLR-induced proliferation of Nb2 cells or Baf3 cells stably transfected with hPRL receptors. It also interacts at 1:1 molar ratio with human prolactin receptor extracellular domain as documented by SEC and SPR (Biacore analysis).

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Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PRLR although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 3 mg/ml and filter sterilization PRLR can be stored at 4C for several weeks. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized PRLR 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 six N-terminal amino acids was determined and was found to be Ala-Arg-Ser-Gln-Val-Thr
Background
Prolactin is a pituitary hormone which takes part in the stimulation of milk production, salt and water regulation, development, growth and reproduction. The primary step in its action is binding a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. PRLR varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL-R consists of at least 3 separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.

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:

GREM1 Human Recombinant

Gremlin-1 isoform 1, CKTSF1B1, DAND2, DRM, GREMLIN, IHG-2, PIG2, GREM1, Cell proliferation-inducing gene 2 protein, Cysteine knot superfamily 1, BMP antagonist 1, DAN domain family member 2, Down-regulated in Mos-transformed cells protein, Increased in high glucose protein 2.

Product # :

PRO-1359

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

GREM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (25-184) and having a molecular mass of 20.7 kDa. GREM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GREM1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
GREM1 belongs to the BMP (bone morphogenic protein) antagonist family. Like BMPs, BMP antagonists comprise cystine knots and usually form homo- and heterodimers. The CAN (cerberus and dan) subfamily of BMP antagonists, to which GREM1 belongs, is characterized by a C-terminal cystine knot with an eight-membered ring. The antagonistic effect of the secreted glycosylated protein is because of its direct binding to BMP proteins. As an antagonist of BMP, GREM1 takes a place in regulating organogenesis, body patterning, and tissue differentiation. In mouse, GREM1 has been shown to convey the sonic hedgehog (SHH) signal from the polarizing region to the apical ectodermal ridge during limb bud outgrowth. Alternatively merged transcript variants encoding different isoforms have been found for this gene.
Synonyms
Gremlin-1 isoform 1, CKTSF1B1, DAND2, DRM, GREMLIN, IHG-2, PIG2, GREM1, Cell proliferation-inducing gene 2 protein, Cysteine knot superfamily 1, BMP antagonist 1, DAN domain family member 2, Down-regulated in Mos-transformed cells protein, Increased in high glucose protein 2.
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 MGSKKKGSQG AIPPPDKAQH NDSEQTQSPQ QPGSRNRGRG QGRGTAMPGE EVLESSQEAL HVTERKYLKR DWCKTQPLKQ TIHEEGCNSR TIINRFCYGQ CNSFYIPRHI RKEEGSFQSC SFCKPKKFTT MMVTLNCPEL QPPTKKKRVT RVKQCRCISI DLD.

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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Quantity :

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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.

More Info

Introduction
Human thyrostimulin ranks among the glycoprotein hormone family. These hormones consist of two subunits, the common alpha- and specific beta-subunits, which associate noncovalently to form a heterodimer. The alpha-subunit combines with four distinct beta-subunits giving rise to four biologically active hormones in human: FSH, LH, TSH, and CG. FSH, LH, and TSH, mainly expressed in the anterior pituitary, are essential for coordinated endocrine regulation in the hypothalamus- pituitary axis and show to activate specific G protein–coupled receptors in the thyroid (TSH receptor) and gonads (LH and FSH receptors), respectively.
The heterodimeric glycoprotein hormones have only been identified in vertebrates and are highly conserved in organisms from primitive rayfin fish (Chondrostei) to human in both primary sequences and functional characteristics.
Corticotroph-derived glycoprotein hormone (CGH), also referred to as thyrostimulin, is a noncovalent heterodimer of glycoprotein hormone alpha 2 (GPHA2) and glycoprotein hormone beta 5 (GPHB5).
Recombinant A2/B5 heterodimeric glycoproteins activates human TSH receptors, but not LH and FSH receptors, and shows high affinity to TSH receptors in a radioligand receptor assay. The heterodimer also stimulates cAMP production and thymidine incorporation by cultured thyroid cells and increases serum thyroxine levels in TSH-suppressed rats in vivo. This new heterodimeric glycoprotein hormone was named as thyrostimulin based on its thyroid-stimulating activity. The expression of thyrostimulin in the anterior pituitary known to express TSH receptors suggested a paracrine mechanism.
Synonyms
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.
Background
What is the molecular weight/Mw of GPHB5 Protein?
GPHB5 Protein has a total Mw of 13.34kDa.

What is the source or expression system of GPHB5 Protein?
Escherichia Coli.

What is the Purity of GPHB5 Protein?
GPHB5 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GPHB5 Protein?
The biological functionality of GPHB5 Protein will be determined in the future.

What is the amino acid sequence of GPHB5 Protein?
MRGSHHHHHH GMASASSGNL RTFVGCAVRE FTFLAKKPGC RGLRITTDAC WGRCETWEKP ILEPPYIEAH HRVCTYNETK QVTVKLPNCA PGVDPFYTYP VAIRCDCGAC STATTECETI.

What applications can GPHB5 Protein be used in?
GPHB5 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GPHB5 Protein?
The endotoxin level is minimal, GPHB5 Protein was purified using conventional chromatography techniques.

Who supplies recombinant GPHB5 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 GPHB5?
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:

LIN28 Human Recombinant

CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.

Product # :

PRO-743

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Description

Recombinant Human LIN28 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (42-209) and having a molecular mass of 21.1 kDa.LIN28 is expressed with a 23 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The LIN28 protein solution (0.5mg/ml) contains 20mM Tris-HCl, pH-8, 10% glycerol, 0.1mM PMSF and 0.1M NaCl.

Purity

Greater than 85.0% as determined by SDS-PAGE

More Info

Introduction
LIN28 plays an important role as a 'translational enhancer', leading specific mRNAs to polysomes and therefore increasing the competence of protein synthesis. LIN28 is a marker of undifferentiated human embryonic stem cells and it enhances the efficiency of the formation of induced pluripotent stem (iPS) cells from human fibroblasts. LIN28 binds to the let-7 pre-miRNA and blocks production of the mature let-7 microRNA in mouse embryonic stem cells. Overexpression of LIN28 is associated with human germ-cell tumors.
Synonyms
CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.
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 SSGLVPRGSHRSMGICKWFN VRMGFGFLSM TARAGVALDP PVDVFVHQSK LHMEGFRSLK EGEAVEFTFK KSAKGLESIR VTGPGGVFCI GSERRPKGKS MQKRRSKGDR CYNCGGLDHH AKECKLPPQP KKCHFCQSIS HMVASCPLKA QQGPSAQGKP TYFREEEEEI HSPTLLPEAQ N.

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 N Human Recombinant

Gamma-crystallin N, Gamma-N-crystallin, CRYGN.

Product # :

PRO-1152

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Description

CRYGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (1-182 a.a) and having a molecular mass of 23.1kDa.CRYGN is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

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

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
Crystallin gamma N (CRYGN) is a member of the Crystallins family. Crystallins are the main proteins of the vertebrate eye lens, where they preserve the transparency and refractive index of the lens. CRYGN is unique in the way that it has both beta and gamma crystallin protein motifs. The CRYGN is differentially controlled after early development, and is involved in cataract creation due to either age-related protein degradation or genetic mutation.
Synonyms
Gamma-crystallin N, Gamma-N-crystallin, CRYGN.
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 MGSHMAQRSG KITLYEGKHF TGQKLEVFGD CDNFQDRGFM NRVNSIHVES GAWVCFNHPD FRGQQFILEH GDYPDFFRWN SHSDHMGSCR PVGMHGEHFR LEIFEGCNFT GQCLEFLEDS PFLQSRGWVK NCVNTIKVYG DGAAWSPRSF GAEDFQLSSS LQSDQGPEEA TTKPATTQPP FLTANL.

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:

Mucosae-Associated Epithelial Chemokine Mouse Recombinant (CCL28)

MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

Product # :

CHM-369

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Description

CCL28 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids and having a molecular mass of 12.6 kDa. The CCL28 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM Phosphate buffer pH-7.4 and 150mM NaCl.

Purity

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

Biological Activity

Determined by its ability to chemoattract mouse lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

More Info

Introduction
CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues.
Synonyms
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CCL28 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL28 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 CCL28 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SEAILPMASS CCTEVSHHVS GRLLERVSSC SIQRADGDCD LAAVILHVKR RRICISPHNR TLKQWMRASE VKKNGRENVC SGKKQPSRKD RKGHTTRKHR TRGTHRHEAS R.
Background
What is the molecular weight/Mw of CCL28 MOUSE Protein?
CCL28 MOUSE Protein has a total Mw of 12.6kDa.

What is the source or expression system of CCL28 MOUSE Protein?
Escherichia Coli.

What is the Purity of CCL28 MOUSE Protein?
CCL28 MOUSE Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL28 MOUSE Protein?
Determined by its ability to chemoattract mouse lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

What is the amino acid sequence of CCL28 MOUSE Protein?
SEAILPMASS CCTEVSHHVS GRLLERVSSC SIQRADGDCD LAAVILHVKR RRICISPHNR TLKQWMRASE VKKNGRENVC SGKKQPSRKD RKGHTTRKHR TRGTHRHEAS R.

What applications can CCL28 MOUSE Protein be used in?
CCL28 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL28 MOUSE Protein?
The endotoxin level is minimal, CCL28 MOUSE Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL28 MOUSE 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 CCL28 MOUSE?
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:

Parathyroid Hormone (7-84) Human Recombinant

Parathyrin, PTH, Parathormone.

Product # :

HOR-011

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

PTH (7-84) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids, having an MW of 8.8kDa. The PTH (7-84) is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

More Info

Introduction
Parathyroid hormone (PTH), or parathormone, is secreted by the parathyroid glands as a polypeptide containing 84 amino acids. It acts to increase the concentration of calcium in the blood, whereas calcitonin (a hormone produced by the parafollicular cells of the thyroid gland) acts to decrease calcium concentration. PTH acts to increase the concentration of calcium in the blood by acting upon parathyroid hormone receptor in three parts of the body: In the bones- It enhances the release of calcium from the large reservoir contained in the bones. Bone resorption is the normal destruction of bone by osteoclasts, which are indirectly stimulated by PTH. Stimulation is indirect since osteoclasts do not have a receptor for PTH; rather, PTH binds to osteoblasts, the cells responsible for creating bone. Binding stimulates osteoblasts to increase their expression of RANKL, which can bind to osteoclast precursors containing RANK, a receptor for RANKL. The binding of RANKL to RANK stimulates these precursors to fuse, forming new osteoclasts which ultimately enhances the resorption of bone. In the kidney- It enhances active reabsorption of calcium from distal tubules and the thick ascending limb. In the intestine- It enhances the absorption of calcium in the intestine by increasing the production of vitamin D and upregulating the enzyme responsible for 1-alpha hydroxylation of 25-hydroxy vitamin D, converting vitamin D to its active form (1,25-dihydroxy vitamin D) which effects the actual absorption of calcium (as Ca2+ ions) by the intestine via calbindin.
Synonyms
Parathyrin, PTH, Parathormone.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PTH (7-84) although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution PTH (7-84) should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized PTH (7-84) in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
LMHNLGKHLN SMERVEWLRK KLQDVHNFVA LGAPLAPRDA GSQRPRKKED NVLVESHEKS LGEADKADVN VLTKAKSQ.
Background
What is the molecular weight/Mw of PARATHORMONE (7-84) Protein?
PARATHORMONE (7-84) Protein has a total Mw of 8.8kDa.

What is the source or expression system of PARATHORMONE (7-84) Protein?
Escherichia Coli.

What is the Purity of PARATHORMONE (7-84) Protein?
PARATHORMONE (7-84) Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of PARATHORMONE (7-84) Protein?
The biological functionality of PARATHORMONE (7-84) Protein will be determined in the future.

What is the amino acid sequence of PARATHORMONE (7-84) Protein?
LMHNLGKHLN SMERVEWLRK KLQDVHNFVA LGAPLAPRDA GSQRPRKKED NVLVESHEKS LGEADKADVN VLTKAKSQ.

What applications can PARATHORMONE (7-84) Protein be used in?
PARATHORMONE (7-84) Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for PARATHORMONE (7-84) Protein?
The endotoxin level is minimal, PARATHORMONE (7-84) Protein was purified using conventional chromatography techniques.

Who supplies recombinant PARATHORMONE (7-84) 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 PARATHORMONE (7-84)?
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:

Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor Human Recombinant

ProSAAS precursor, Proprotein convertase subtilisin/kexin type 1 inhibitor, PROSAAS; SAAS, PCSK1N.

Product # :

PRO-1819

Price :

Quantity :

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Shipped with Ice Packs

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Description

PCSK1N Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 251 amino acids (34-260) and having a molecular mass of 26.6 kDa.PCSK1N is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PCSK1N solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor (PCSK1N) takes part in the control of the neuroendocrine secretory pathway. PCSK1N inhibits prohormone convertase 1, which regulates the proteolytic cleavage of neuroendocrine peptide precursors. PCSK1Nslows down convertase-mediated processing of proopiomelanocortin and proenkephalin and also monitors the intracellular timing of PCSK1.
Synonyms
ProSAAS precursor, Proprotein convertase subtilisin/kexin type 1 inhibitor, PROSAAS; SAAS, PCSK1N.
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 MGSMARPVKE PRGLSAASPP LAETGAPRRF RRSVPRGEAA GAVQELARAL AHLLEAERQE RARAEAQEAE DQQARVLAQL LRVWGAPRNS DPALGLDDDP DAPAAQLARA LLRARLDPAA LAAQLVPAPV PAAALRPRPP VYDDGPAGPD AEEAGDETPD VDPELLRYLL GRILAGSADS EGVAAPRRLR RAADHDVGSE LPPEGVLGAL LRVKRLETPA PQVPARRLLP 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:

Urocortin 3 Human Recombinant

Stresscopin, urocortin-iii.

Product # :

HOR-056

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

The UCN3Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The UCN3His-Tagged Fusion Protein, produced in E. coli, is a 20kDa protein containing 161 amino acid residues of the UCN3Human, 1-161 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

Synonyms
Stresscopin, urocortin-iii.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized UCN3at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Background
Urocortin 3 also known as UCN3 is a part of the corticotropin-releasing factor (CRF) family of peptides, which are involved in metabolism, stress response and neuroendocrine regulation. UCN3 exerts its biological effects through interactions with CRFR2. UCN3 takes a main part in mediating few important biological processes, specially those associated with energy metabolism, stress response and the regulation of the hypothalamic-pituitary-adrenal (HPA) axis. UCN3 expressed mainly in the brain in areas such as the hypothalamus, as well as in peripheral tissues, including the heart and adipose tissue.
What is the molecular weight/Mw of UCN3 HUMAN Protein?
UCN3 HUMAN Protein has a total Mw of 20kDa.

What is the source or expression system of UCN3 HUMAN Protein?
Escherichia Coli.

What is the Purity of UCN3 HUMAN Protein?
UCN3 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of UCN3 HUMAN Protein?
The biological functionality of UCN3 HUMAN Protein will be determined in the future.

What applications can UCN3 HUMAN Protein be used in?
UCN3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for UCN3 HUMAN Protein?
The endotoxin level is minimal, UCN3 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:

Melanoregulin Human Recombinant

Melanoregulin, DSU, Dilute Suppressor Protein Homolog, WDT2, Whn-Dependent Transcript 2.

Product # :

PRO-1885

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

MREG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-214 a.a) and having a molecular mass of 27.3kDa.MREG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MREG protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
Melanoregulin (MREG) takes part in membrane fusion and in regulating the biogenesis of disk membranes of photoreceptor rods. MREG is expressed in photoreceptor cells as two isoforms as a result of alternative splicing. MREG interacts with Peripherin-2, a photoreceptor specific tetraspanin protein which is required to preserve normal cell structure during the renewal process of membrane fusion. Moreover, MREG plays a part in the incorporation of pigments into hair.
Synonyms
Melanoregulin, DSU, Dilute Suppressor Protein Homolog, WDT2, Whn-Dependent Transcript 2.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGLRDWL RTVCCCCGCE CLEERALPEK EPLVSDNNPY SSFGATLVRD DEKNLWSMPH DVSHTEADDD RTLYNLIVIR NQQAKDSEEW QKLNYDIHTL RQVRREVRNR WKCILEDLGF QKEADSLLSV TKLSTISDSK NTRKAREMLL KLAEETNIFP TSWELSERYL FVVDRLIALD AAEEFFKLAR RTYPKKPGVP CLADGQKELH YLPFPSP

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:

P-selectin Human Recombinant

P-selectin, Granule membrane protein 140, GMP-140, PADGEM, Leukocyte-endothelial cell adhesion molecule 3, LECAM3, CD62 antigen-like family member P, CD62P antigen, SELP, GMRP, GRMP, CD62, PSEL, CD62P, GMP140, FLJ45155.

Product # :

PRO-382

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

P-Selectin Human Recombinant is expressed in E. coli containing 566 amino acids 197-761 fused to an amino terminal hexahistidine tag.

Source

Escherichia Coli.

Formulation

P-Selectin is supplied in 50% Glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.
Single band on Western Blot.

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Introduction
P-Selectin also called Platelet Alpha-Granule Membrane Protein, CD62, and Granulocyte Membrane Protein GRMP belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Pselectin is expressed transiently on the surface of activated platelets and endothelial cells. P-Selectin is a 140 kDa protein which is stored in the alpha-granules of platelets and Weibel-Palade bodies of endothelial cells. Secreted P-selectin is thought to play a key role in the adhesion of platelets to monocytes and neutrophils during an inflammatory response. P-Selectin is a calcium-dependent receptor that binds to sialylated forms of Lewis blood group carbohydrate antigens on neutrophils and monocytes. Levels of P-Selectin may be elevated in a number of pathological conditions.
Synonyms
P-selectin, Granule membrane protein 140, GMP-140, PADGEM, Leukocyte-endothelial cell adhesion molecule 3, LECAM3, CD62 antigen-like family member P, CD62P antigen, SELP, GMRP, GRMP, CD62, PSEL, CD62P, GMP140, FLJ45155.
Physical Appearance
Sterile Filtered liquid formulation.
Stability
Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
Applications
P-Selectin can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
The biological activity of this product has not yet been tested.

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:

Proopiomelanocortin Human Recombinant

Pro-opiomelanocortin, POMC, LPH, MSH, NPP, POC, ACTH, CLIP.

Product # :

PRO-236

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

POMC produced in E.Coli is a single, non-glycosylated polypeptide chain containing 262 amino acids (27-267 a.a) and having a molecular mass of 28.9kDa (molecular weight on SDS-PAGE will appear higher).POMC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

POMC protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.5), 1mM DTT, 50% glycerol, 0.1mM PMSF, 0.1M Imidazole and 0.2M NaCl.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Pro-opiomelanocortin preproprotein (POMC) is a polypeptide hormone precursor which experiences extensive, tissue-specific, post-translational processing via cleavage by subtilisin-like enzymes known as prohormone convertases. POMC regulates the corticosteroid production in the adrenal cortex. Furthermore, POMC is cleaved into ten hormone chains named NPP, g-MSH, ACTH, a-MSH, CLIP, Lipotropin b, Lipotropin g, b-MSH,b endorphin and Met-enkephalin. POMC gene defects are the cause of POMC deficiency, which is characterized by red hair and adrenal insufficiency.
Synonyms
Pro-opiomelanocortin, POMC, LPH, MSH, NPP, POC, ACTH, CLIP.
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 MWCLESSQCQ DLTTESNLLE CIRACKPDLS AETPMFPGNG DEQPLTENPR KYVMGHFRWD RFGRRNSSSS GSSGAGQKRE DVSAGEDCGP LPEGGPEPRS DGAKPGPREG KRSYSMEHFR WGKPVGKKRR PVKVYPNGAE DESAEAFPLE FKRELTGQRL
REGDGPDGPA DDGAGAQADL EHSLLVAAEK KDEGPYRMEH FRWGSPPKDK RYGGFMTSEK SQTPLVTLFK NAIIKNAYKK GE.

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:

Egl Nine Homolog 3 Human Recombinant

Egl nine homolog 3 (C. elegans), Hypoxia-inducible factor prolyl hydroxylase 3, Prolyl hydroxylase domain-containing protein 3, HIF-PH3, PHD3, egl nine-like protein 3 isoform, HIF prolyl hydroxylase 3, EC 1.14.11.29, HPH-1, HPH-3.

Product # :

PRO-1143

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

EGLN3 Human Recombinant produced in E. coli is a single polypeptide chain containing 263 amino acids (1-239) and having a molecular mass of 29.8 kDa.EGLN3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The EGLN3 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 300mM NaCl, 5mM DTT, 2mM EDTA and 50% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Egl Nine Homolog 3 (EGLN3) belongs to the EGLN family of prolyl hydroxylases. EGLN3 catalyzes hydroxylation of the ? subunit of hypoxia-inducible factor-?, which targets hypoxia-inducible factor-? for ubiquitination by a ubiquitin ligase complex containing the von Hippel-Lindau (VHL) tumor suppressor. EGLN3 is the most significant isozyme in limiting physiological activation of HIFs (especially HIF2A) in hypoxia. EGLN3 is activated in cardiovascular cells and Hela cells after exposure to hypoxia. In addition, EGLN3 hydroxylates PKM2 in hypoxia, thus limiting glycolysis. Under normoxia, EGLN3 hydroxylates and regulates the stability of ADRB2. EGLN3 is inhibited by polynitrogen compounds possibly by chelation to Fe2+ ions.
Synonyms
Egl nine homolog 3 (C. elegans), Hypoxia-inducible factor prolyl hydroxylase 3, Prolyl hydroxylase domain-containing protein 3, HIF-PH3, PHD3, egl nine-like protein 3 isoform, HIF prolyl hydroxylase 3, EC 1.14.11.29, HPH-1, HPH-3.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMPLGHI MRLDLEKIAL EYIVPCLHEV GFCYLDNFLG EVVGDCVLER VKQLHCTGAL RDGQLAGPRA GVSKRHLRGD QITWIGGNEE GCEAISFLLS LIDRLVLYCG SRLGKYYVKE RSKAMVACYP GNGTGYVRHV DNPNGDGRCI TCIYYLNKNW DAKLHGGILR IFPEGKSFIA DVEPIFDRLL FFWSDRRNPH EVQPSYATRY AMTVWYFDAE ERAEAKKKFR NLTRKTESAL TED

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:

Kisspeptin-10

Product # :

HOR-044

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Kisspeptin-10 Synthetic is a single, non-glycosylated polypeptide chain containing 10 amino acids, having a molecular mass of 1302 Dalton and a Molecular formula of C63H83N17O14 .

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 Kisspeptin-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Kisspeptin-10 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 Kisspeptin-10 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-Tyr-Asn-Trp-Asn-Ser-Phe-Gly-Leu-Arg-Phe-NH2.
Background
Kisspeptin-10, a peptide derived from the Kisspeptin gene (KISS1), has emerged as a key player in the regulation of reproductive physiology. The peptide is known for its potent ability to stimulate the release of gonadotropin-releasing hormone (GnRH), a crucial factor in the control of the hypothalamic-pituitary-gonadal axis. The pivotal role of kisspeptin-10 in orchestrating the onset of puberty and the regulation of the menstrual cycle highlights its significance in reproductive health. This research aims to delve into the multifaceted functions of kisspeptin-10, shedding light on its physiological roles and potential applications in reproductive disorders.
The primary objective of this study is to comprehensively explore the effects of kisspeptin-10 on the reproductive system. In vitro and in vivo assays will be conducted to investigate the impact of kisspeptin-10 on GnRH release and subsequent gonadotropin secretion. The interactions between kisspeptin-10 and its receptor, G protein-coupled receptor 54 (GPR54), will be explored using binding assays, potentially unraveling novel signaling pathways activated by this interaction.
The second objective is to investigate the potential therapeutic applications of kisspeptin-10 in reproductive disorders. Clinical studies and animal models will be utilized to assess the efficacy of kisspeptin-10 in stimulating ovulation, particularly in cases of infertility caused by hypothalamic dysfunction. Furthermore, the potential of kisspeptin-10 in regulating conditions like polycystic ovary syndrome (PCOS) and hypogonadotropic hypogonadism will be explored.
The third objective is to elucidate the molecular mechanisms underlying the actions of kisspeptin-10. Transcriptomic and proteomic analyses will be employed to identify genes and proteins regulated by kisspeptin-10 stimulation. This information could reveal novel downstream effectors of kisspeptin-10 signaling, contributing to a more comprehensive understanding of its role in reproductive physiology.
By delving into the complexities of kisspeptin-10, this research aims to provide insights into its multifunctional roles in reproductive health and expand its potential therapeutic applications. The findings from this study may pave the way for the development of targeted interventions for reproductive disorders, potentially improving the quality of life for individuals affected by these conditions.

What is the molecular weight/Mw of KISSPEPTIN-10 Protein?
KISSPEPTIN-10 Protein has a total Mw of 1.302kDa.

What is the Purity of KISSPEPTIN-10 Protein?
KISSPEPTIN-10 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of KISSPEPTIN-10 Protein?
The biological functionality of KISSPEPTIN-10 Protein will be determined in the future.

What is the amino acid sequence of KISSPEPTIN-10 Protein?
H-Tyr-Asn-Trp-Asn-Ser-Phe-Gly-Leu-Arg-Phe-NH2.

What applications can KISSPEPTIN-10 Protein be used in?
KISSPEPTIN-10 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for KISSPEPTIN-10 Protein?
The endotoxin level is minimal, KISSPEPTIN-10 Protein was purified using conventional chromatography techniques.

Who supplies KISSPEPTIN-10 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 KISSPEPTIN-10?
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:

ProInsulin C-Peptide Analogue Human Recombinant

Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.

Product # :

CYT-1120

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

ProInsulin C-Peptide Analogue Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 35 amino acid and having a molecular mass of approximately 3.6kDa.ProInsulin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

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Introduction
Insulin decreases blood glucose concentration. Insulin increases cell permeability to monosaccharides, amino acids and fatty acids. Insulin accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
Synonyms
Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized ProInsulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ProInsulin C-Peptide Analogue 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 ProInsulin C-Peptide Analogue in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
RREAEDLQVG QVELGGGPGA GSLQPLALEG SLQKR.

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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