Search results
1000 results found for “Glucagon”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
Leptin tA Mouse, PEG (D23L)Description:
Leptin Triple Antagonist (D23L) Pegylated Mouse Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1242Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Leptin Antagonist Triple Mutant D23L Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus. The Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant. The Mouse Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Mouse Leptin triple anatagonist runs as a 48 kDa. Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Mouse Leptin triple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Leptin Antagonist Triple Mutant D23L Mouse Recombinant is capable of stimulating proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is only slightly lower than the non-pegylated recombinant mouse leptin but in vivo it has profound weight reducing effect (as compared to the non-pegylated recombinant mouse leptin), resulting mainly from reduced food intake.
Citations
More Info
-
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C 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 Leptin Antagonist Triple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
-
Background
Leptin is a hormone which mainly produced by adipocytes . Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin effects mainly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor is found on a wide range of cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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.
- View Data Sheet
Name :
PYGL HumanDescription:
Phosphorylase, Glycogen, Liver Human Recombinant
GSD6, Glycogen phosphorylase, liver form.
Product # :
ENZ-675Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
PYGL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 879 amino acids (1-847 a.a) and having a molecular mass of 100.7kDa.PYGL is fused to a 32 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PYGL protein solution (0.25mg/ml) in phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Glycogen phosphorylase (PYGL) converts from inactive phosphorylase B to active phosphorylase A by phosphorylation of serine residue 15. Activity of the PYGL enzyme is further regulated by numerous allosteric effectors and hormonal controls. The liver isozyme supplies the glycemic demands of the body in general whereas the brain and muscle isozymes supply just those tissues.
-
Synonyms
GSD6, Glycogen phosphorylase, liver form.
-
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 MGSEFELRRQ ASMAKPLTDQ EKRRQISIRG IVGVENVAEL KKSFNRHLHF TLVKDRNVAT TRDYYFALAH TVRDHLVGRW IRTQQHYYDK CPKRVYYLSL EFYMGRTLQN TMINLGLQNA CDEAIYQLGL DIEELEEIEE DAGLGNGGLG RLAACFLDSM ATLGLAAYGY GIRYEYGIFN QKIRDGWQVE EADDWLRYGN PWEKSRPEFM LPVHFYGKVE HTNTGTKWID TQVVLALPYD TPVPGYMNNT VNTMRLWSAR APNDFNLRDF NVGDYIQAVL DRNLAENISR VLYPNDNFFE GKELRLKQEY FVVAATLQDI IRRFKASKFG STRGAGTVFD AFPDQVAIQL NDTHPALAIP ELMRIFVDIE KLPWSKAWEL TQKTFAYTNH TVLPEALERW PVDLVEKLLP RHLEIIYEIN QKHLDRIVAL FPKDVDRLRR MSLIEEEGSK RINMAHLCIV GSHAVNGVAK IHSDIVKTKV FKDFSELEPD KFQNKTNGIT PRRWLLLCNP GLAELIAEKI GEDYVKDLSQ LTKLHSFLGD DVFLRELAKV KQENKLKFSQ FLETEYKVKI NPSSMFDVQV KRIHEYKRQL LNCLHVITMY NRIKKDPKKL FVPRTVIIGG KAAPGYHMAK MIIKLITSVA DVVNNDPMVG SKLKVIFLEN YRVSLAEKVI PATDLSEQIS TAGTEASGTG NMKFMLNGAL TIGTMDGANV EMAEEAGEEN LFIFGMRIDD VAALDKKGYE AKEYYEALPE LKLVIDQIDN GFFSPKQPDL FKDIINMLFY HDRFKVFADY EAYVKCQDKV SQLYMNPKAW NTMVLKNIAA SGKFSSDRTI KEYAQNIWNV EPSDLKISLS NESNKVNGN.
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.
- View Data Sheet
Name :
Exendin 4Description:
Exendin-4 Recombinant
Product # :
HOR-269Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Exendin-4 Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 39 amino acids and having a molecular mass of approximately 4.2kDa. Exendin-4 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 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
1. Regulates Glucose levels rapidly
2. Reduces Insulin resistance
3. Reduces Glucagon4. Stimulates beta cell growth production.
Citations
More Info
-
Introduction
Exedin-4 Recombinant is a like peptide-1 receptor agonist. The native hormone is produced in the gut of Gila monster Heloderma suspectrum (a type of reptile found in the desert) that stimulates production without causing threateningly low blood sugar, which can occur after using some anti-diabetes products. Recently, researchers used extracted saliva from gila monsters to create an unprecedented breakthrough in Diabetes Type 2 treatment. Unlike other products taken for type 2 diabetes, Exedin-4 has not been linked with weight gain and actually resulted in weight loss, according to the researchers. Exedin-4 enhances glucose-dependant secretion, suppresses inappropriately elevated secretion and slows gastric emptying in vivo. It also promotes B-cell proliferation and neogenesis in vitro and in animal models. Exedin-4 stimulates an increase in acinar cAMP, without stimulating the release of amylase.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Exendin Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Exendin-4 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Exendin Recombinant in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
HGEGTFTSDL SKQMEEEAVR LFIEWLKNGG PSSGAPPPS.
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.
- View Data Sheet
Name :
Leptin qA Human, PEGDescription:
Leptin Quadruple Antagonist Pegylated Human Recombinant
Product # :
CYT-1251Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Leptin Pegylated Quadruple Antagonist Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and an additional Ala at N-terminus acids. The Human Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Human Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Human Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/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
Human Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated human leptin antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated human leptin antagonist), resulting mainly from increased food intake. The in vivo activity of human pegylated super leptin antagonist was compared to that of human pegylated leptin antagonist is 9-27 fold higher.
Citations
More Info
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Human Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of Human pegylated leptin antagonist and filter sterilization Human pegylated leptin antagonist can be stored at 4°C 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 Human Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
-
Background
Leptin is a~16 kDa protein which is encoded by the obese gene. Leptin is a hormone which participates in regulating body weight, reproductive function and metabolism. leptin is expressed predominantly by adipocytes, which supports 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.
-
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Gliadin Gamma WheatDescription:
Gliadin Gamma Wheat Recombinant
Product # :
PRO-2148Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
Recombinant Wheat Gliadin Gamma protein produced in E.Coli and fused to a 6 His Tag at C-terminus, having a theoretical Mw of 37945.14 Dalton, pI 7.70.Purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
Gliadin Gamma protein solution (1mg/ml) in 10mM Tris-HCl pH 7.2.
Purity
Protein is >90% pure.
Citations
More Info
-
Introduction
Wheat Gliadin and related gluten components from barley, rye and possibly oats can cause an abnormal immune response called Celiac disease which is a chronic gastrointestinal disorder. Celiac disease characteristics are flattening of the jejunal mucosa and intestinal lesions of variable severity in hereditarily inclined individuals. Even though Celiac disease is not a classic autoimmune disease it is related to anti-tissue transglutaminase antibodies and gliadin antibodies tests are most recommended in screening populations at risk for CD and other gluten-sensitive enteropathies. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Gliadin Gamma although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Amino Acid Sequence
MKTLLILTILAMAITIGTANIQVDPSGQVQWLQQQLVPQLQQPLSQQPQQTFPQPQQTFPH
QPQQQVPQPQQPQQPFLQPQQPFPQQPQQPFPQTQQPQQPFPQQPQQPFPQTQQPQQ
PFPQQPQQPFPQTQQPQQPFPQLQQPQQPFPQPQQQLPQPQQPQQSFPQQQRPFIQPSL
QQQLNCKNILLQQSKPASLVSSLWSIIWPQSDCQVMRQQCCQQLAQIPQQLQCAAIHSVVH
SIIMQQQQQQQQQQGIDIFLPLSQHEQVGQGSLVQGQGIIQPQQPAQLEAIRSLVLQTLPSM
CNVYVPPECSIMRAPFASIVAGIGGQHHHHHH.
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.
- View Data Sheet
Name :
SCGN RatDescription:
Secretagogin Rat Recombinant
SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, Secretagogin.
Product # :
PRO-657Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
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.
Citations
More Info
-
Introduction
SCGN is a secreted calcium-binding protein which is found in the cytoplasm. It is related to calbindin D-28K and calretinin. Secretagogin is involved in KCL-stimulated calcium flux and cell proliferation.
Secretagogin plays a role in human non-functional pituitary adenomas. -
Synonyms
SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, 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.
- View Data Sheet
Name :
Leptin qA Rat, PEGDescription:
Leptin Quadruple Antagonist, Pegylated Rat Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1241Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Leptin Pegylated Quadruple Antagonist Rat Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids. The Rat Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Rat Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Rat Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/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
Rat Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro.
Citations
More Info
-
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Rat Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of rat pegylated leptin antagonist and filter sterilization rat pegylated leptin antagonist can be stored at 4°C 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 Rat Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
-
Background
Leptin is a hormone which mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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.
- View Data Sheet
Name :
Adiponectin Porcine, HEKDescription:
Adiponectin Porcine Recombinant, HEK derived
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-696Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
The Acrp30 Porcine Recombinant contains a total of 238 amino acids having a molecular Mass of 26kDa. The Porcine Adiponectin is fused to a 13 amino acid long N-terminal FLAG tag.
Source
HEK293 (Human Embryonic Kidney cell line).
Formulation
Sterile filtered and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.
Purity
Greater than 90% as determined by SDS PAGE.
Citations
More Info
-
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.
-
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 and let the lyophilized pellet dissolve completely.
-
Amino Acid Sequence
HVDYKDDDDK PAGETTEKPG ALLPMPKGAC AGWMAGIPGH PGHNGTPGRD GRDGVPGEKG EKGDTGLTGP KGDTGESGVT GVEGPRGFPG IPGRKGEPGE SAYVYRSAFS VGLETRVTVP NMPIRFTKIF YNQQNHYDVT TGKFHCNIPG LYYFSFHITV LKDVKVSLYK DKAVLFTYDQ QDKNVDQASG VLLYLEKGDQ WLQAYGDEEN GVYADNVNDS FTGFLLYHNIE.
-
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 26kDa.
What is the source or expression system of ADIPONECTIN Protein?
HEK293
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?
HVDYKDDDDK PAGETTEKPG ALLPMPKGAC AGWMAGIPGH PGHNGTPGRD GRDGVPGEKG EKGDTGLTGP KGDTGESGVT GVEGPRGFPG IPGRKGEPGE SAYVYRSAFS VGLETRVTVP NMPIRFTKIF YNQQNHYDVT TGKFHCNIPG LYYFSFHITV LKDVKVSLYK DKAVLFTYDQ QDKNVDQASG VLLYLEKGDQ WLQAYGDEEN GVYADNVNDS FTGFLLYHNIE.
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.
- View Data Sheet
Name :
GHK-CuDescription:
GHK-Cu
Copper Tripeptide-1
Product # :
HOR-063Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
- Citations
Description
GHK-Cu is a synthetic single, non-glycosylated polypeptide chain containing 3 amino acids, having a molecular mass of 401.91 Dalton and a Molecular formula of C14H22N6O4Cu.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
Citations
More Info
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized GHK-Cu although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GHK-Cu 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 GHK-Cu in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
Gly-His-Lys.
-
Background
GHK-Cu is located in human plasma and has an ability to modify gene expression to a healthier state, influencing more than 4,000 human genes. GHK-Cu can change pathological gene expression to a healthy mode, mainly in chronic conditions as metastatic cancer, COPD and Ulcerative Colitis. GHK-Cu was discovered to be effective in systemic repair and neuroprotection.
What is the molecular weight/Mw of GHK-CU Protein?
GHK-CU Protein has a total Mw of 0.40kDa.
What is the Purity of GHK-CU Protein?
GHK-CU Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of GHK-CU Protein?
The biological functionality of GHK-CU Protein will be determined in the future.
What is the amino acid sequence of GHK-CU Protein?
Gly-His-Lys.
What applications can GHK-CU Protein be used in?
GHK-CU Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GHK-CU Protein?
The endotoxin level is minimal, GHK-CU Protein was purified using conventional chromatography techniques.
Who supplies GHK-CU 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 GHK-CU?
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.
- View Data Sheet
Name :
BTC Human, HEKDescription:
Betacellulin Human Recombinant, HEK
Betacellulin isoform 1, Probetacellulin, Betacellulin, BTC
Product # :
CYT-1188Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
BTC Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (32-111 a.a) containing 86 amino acids and having a molecular mass of 9.8kDa.BTC is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
BTC protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
ED50 range is ≤ 0.5ng/ml. It is measured by cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells.
Citations
More Info
-
Introduction
BTC is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are mediated by the EGF receptor and other related receptors.
-
Synonyms
Betacellulin isoform 1, Probetacellulin, Betacellulin, BTC
-
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
DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY HHHHHH
-
Background
What is the molecular weight/Mw of BETACELLULIN Protein?
BETACELLULIN Protein has a total Mw of 9.8kDa.
What is the source or expression system of BETACELLULIN Protein?
HEK293 cells.
What is the Purity of BETACELLULIN Protein?
BETACELLULIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BETACELLULIN Protein?
ED50 range is ≤ 0.5ng/ml. It is measured by cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells.
What is the amino acid sequence of BETACELLULIN Protein?
DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY HHHHHH
What applications can BETACELLULIN Protein be used in?
BETACELLULIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BETACELLULIN Protein?
The endotoxin level is minimal, BETACELLULIN 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.
- View Data Sheet
Name :
GHRL HumanDescription:
Ghrelin Human Recombinant
Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.
Product # :
HOR-294Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
Ghrelin Human Recombinant contains 115 amino acids (24-117 a.a.) and a total molecular mass of 12.8 kDa. The GHRL is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Ghrelin protein solution contains 20mM Tris-HCl, pH-8 & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Obestatin is a hormone that is produced in the cells lining the stomach and small intestine of several mammals including humans; it drastically reduces appetite in mice and is expected to do the same in humans. Obestatin is a peptide hormone - a relatively small protein. It is encoded by the same gene that also encodes ghrelin, a peptide hormone that increases appetite. The protein produced by that gene breaks into two smaller peptides, ghrelin and obestatin. Ghrelin is an endogenous ligand for the growth hormone secretagogue receptor and is involved in regulating growth hormone release. Ghrelin is derived from a preprohormone called preproghrelin, which also generates a second peptide called obestatin. Ghrelin is an endogenous ligand for the orphan G protein-coupled receptor GPR39 and is involved in satiety and decreased food intake.
-
Synonyms
Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.
-
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 MGSSFLSPEH QRVQQRKESK KPPAKLQPRA LAGWLRPEDG GQAEGAEDEM EVRFNAPFDV GIKLSGVQYQ QHSQALGKFL QDILWEEAKE APADK.
-
Background
What is the molecular weight/Mw of GHRELIN HUMAN Protein?
GHRELIN HUMAN Protein has a total Mw of 12.8kDa.
What is the source or expression system of GHRELIN HUMAN Protein?
Escherichia Coli.
What is the Purity of GHRELIN HUMAN Protein?
GHRELIN HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of GHRELIN HUMAN Protein?
The biological functionality of GHRELIN HUMAN Protein will be determined in the future.
What is the amino acid sequence of GHRELIN HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSSFLSPEH QRVQQRKESK KPPAKLQPRA LAGWLRPEDG GQAEGAEDEM EVRFNAPFDV GIKLSGVQYQ QHSQALGKFL QDILWEEAKE APADK.
What applications can GHRELIN HUMAN Protein be used in?
GHRELIN HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GHRELIN HUMAN Protein?
The endotoxin level is minimal, GHRELIN 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.
- View Data Sheet
Name :
TerlipressinDescription:
Terlipressin
Product # :
HOR-287Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
- Citations
Description
Terlipressin contains 12 amino acids Gly-Gly-Gly-c[Cys-Tyr-Phe-Gln-Asn-Cys]-Pro-Lys-Gly-NH2 and having a molecular weight of 1227.37 Dalton.
Formulation
The protein (1 mg/ml) was lyophilized with no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
-
Introduction
Terlipressin is similar to a naturally occurring hormone present in the body, known as antidiuretic hormone (ADH) or vasopressin. ADH has two main effects in the body. Firstly, it causes narrowing of blood vessels (vasoconstriction), thereby limiting blood flow to a particular area of the body. It also acts on receptors in the kidney to retain water in the body, which helps to prevent excessive loss of water in the urine. Terlipressin is commonly used to stop bleeding of varices in the food pipe (oesophagus). Varices are fragile distended veins that can occur in various parts of the body such as the oesophagus. This is caused by an increase in blood pressure in certain diseases such as severe liver disease. These fragile varices can rupture and lead to life threatening bleeding. Terlipressin is therefore given to narrow blood vessels, and so restricting blood flow to the varices and stopping the bleeding.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Terlipressin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Terlipressin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Terlipressin18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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.
- View Data Sheet
Name :
Globular Adiponectin HumanDescription:
Globular Adiponectin Human Recombinant
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-615Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
gAcrp30 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 145 amino acids and having a molecular mass of 16.7kDa. The gAcrp30 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Sterile filtered and lyophilized from 10mM sodium phosphate & 0.5mM DTT, pH 7.5.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
gAcrp30 activity is determined by its ability to inhibit the proliferation of mouse M1 cells. The expected ED50 for this effect is 669ng/ml, corresponding to a specific activity of 1.5x103units/mg.
Citations
More Info
-
Introduction
gAcrp30 globular protein, exists as a result of proteolytic processing of adiponectin. Adiponectin is manufactured and secreted solely by adipocytes, and is a highly obtained plasma protein, accounting for up to 0.05% of total serum protein. Similar to Adiponectin, gAcrp30 is able of lowering hyperglycemia and reversing INS resistance. In addition, gAcrp30 is an significant protein that is involved in promoting fat loss by signaling muscle to absorb and burn Free-Fatty Acids. AdipoR1 & AdipoR2 are the 2 signaling receptors for adiponectin and gAcrp30 that were recently been identified.
-
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
-
Stability
For long term, 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 two weeks.
-
Solubility
We recommended reconstituting gAcrp30 at a concentration of 0.1mg per ml with 10mM sodium phosphate & 0.5mM DTT, pH 7.5. which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MKGEPGEGAY VYRSAFSVGL ETYVTIPNMP IRFTKIFYNQ QNHYDGSTGK FHCNIPGLYY FAYHITVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTN.
-
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 16.7kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
gAcrp30 activity is determined by its ability to inhibit the proliferation of mouse M1 cells. The expected ED50 for this effect is 669ng/ml, corresponding to a specific activity of 1.5x103units/mg.
What is the amino acid sequence of ADIPONECTIN Protein?
MKGEPGEGAY VYRSAFSVGL ETYVTIPNMP IRFTKIFYNQ QNHYDGSTGK FHCNIPGLYY FAYHITVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTN.
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.
- View Data Sheet
Name :
Gly m 4.0101Description:
Stress-Induced Protein SAM22 Recombinant
Stress-induced protein SAM22, Starvation-associated message 22, Gly m 4.
Product # :
PRO-2278Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
Recombinant Stress-Induced Protein SAM22 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 19,484 Dalton. Gly m 4.0101 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
Gly m 4.0101 is supplied in in 20mM HEPES buffer pH-7.9 and 6M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Stress-Induced Protein SAM22 (Gly m 4.0101) causes an allergic reaction in humans. Gly m 4 is the main soy allergen for patients allergic to birch pollen with soy allergy.
-
Synonyms
Stress-induced protein SAM22, Starvation-associated message 22, Gly m 4.
-
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. Avoid multiple freeze-thaw cycles.
-
Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
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.
- View Data Sheet
Name :
Insulin Human (20-110)Description:
Insulin (20-110 a.a) Human Recombinant
Product # :
CYT-1237Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
The Insulin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Insulin His-Tagged Fusion Protein, produced in E. coli, is a 13kDa protein containing 91 amino acid residues of the Insulin Human, 20-110 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized Insulin at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
-
Amino Acid Sequence
MALWMRLLPL LALLALWGPD PAAAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN
-
Background
Insulin participates in the metabolism of carbohydrates, proteins and fats by regulating glucose homeostasis in the body. Insulin decreases blood glucose concentration. Insulin hormone facilitates the uptake of glucose into cells, mainly in muscle and fat tissues, and stimulates the liver to store glucose as glycogen. Insulin also inhibits the production of gluconeogenesis and promotes the synthesis of proteins and lipids. Insulin increases cell permeability to monosaccharides, fatty acids and amino acids. Insulin accelerates glycolysis, the pentose phosphate cycle and glycogen synthesis in liver.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ElcatoninDescription:
Elcatonin
Product # :
HOR-302Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Elcatonin Synthetic is a single, non-glycosylated polypeptide chain containing 31 amino acids, having a molecular mass of 3363.2 Dalton and a Molecular formula of C148H244N42O47.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 93.3% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Biological Activity (based on net peptide) was found to be 6695.2 IU/mg.Citations
More Info
-
Introduction
Elcatonin is a Calcitonin derivative which is transformed from eel´s calcitonin by changing the S-S bond into the stable C-N bond. It inhibits the absorption and autolysis of bones, thus leads to blood calcium descending. In addition, it inhibits the bone salts dissolving and transferring and promotes the excretion of calcium and phosphorus in urine. Meanwhile, it inhibits renal tubules reabsorbing calcium, phosphorus and sodium and keeps blood calcium at normal level. It is mainly used for remitting or eliminating the pain caused by Osteoporosis.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Elcatonin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Elcatonin 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 Elcatonin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
Ser-Asn-Leu-Ser-Thr-Asu-Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn-Val-Gly-Ala-Gly-Thr-Pro-NH2.
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.
- View Data Sheet
Name :
Leptin tA Human, PEGDescription:
Leptin Antagonist Triple Mutant Human Recombinant, Pegylated
Product # :
CYT-702Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Pegylated Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 35.6kDa, Leptin was mutated, resulting in L39A/D40A/F41A. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. Leptin Antagonist Triple Mutant Human Recombinant is Mono-Pegylated with 20kDa PEG and was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (0.65mg/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
Capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake. Its in vivo activity compared to that of PEG-MLA is 9-27 fold higher.Citations
More Info
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized PEG-SHLA although stable at room temperature for several weeks, should be stored desiccated below - 20C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml of PEG-SHLA and filter sterilization mLEP mutant 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 Leptin Antagonist Triple Mutant pegylated Human Recombinant 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.
-
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GLC8 YeastDescription:
GLC8 Yeast Recombinant
Protein GLC8, GLC8, YMR311C, YM9924.03C.
Product # :
PRO-540Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
GLC8 Yeast (Saccharomyces cerevisiae) Recombinant produced in E.coli is a single, glycosylated polypeptide chain containing 265 amino acids (1-229) and having a molecular mass of 30.7 kDa (molecular size on SDS-PAGE will appear higher). The GLC8 is fused to a 35 amino acid His Tag at N-Terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT, and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
GLC8 is a regulatory subunit of protein phosphatase 1 (Glc7p). GLC8 plays a role in glycogen metabolism and chromosome segregation, and regulates Glc7p activity through conformational alteration; ortholog of the mammalian protein phosphatase inhibitor 2. Under regular conditions, GLC8 triggers GLC7, but when GLC8 is over epxressed, it inhibits Glc7p function. GLC8 is activated upon phosphoylation by Pho85p complexed with four cyclins (Pcl6p, Pcl7p, Pcl8p, or Pcl10p).
-
Synonyms
Protein GLC8, GLC8, YMR311C, YM9924.03C.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMGGI LKNPLALSPE QLAQQDPETL EEFRRQVYEN TQKNAKLTSH KRNIPGLDNT KEEGEIIGTS STFLPKDTLS LKHEQDMLAK MTPEERVQWN QRNLAENEIT KKQFQDIHID EPKTPYQGAV DPHGEYYRVD DDEDEDNSDK KPCQVANDDI DDLSLGEPEF EIKENKQPDF ETNDENDEDS PEARHKKFEE MRKKHYDVRA IFNKKSREAL KDEDEDEDDS TTKEP.
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.
- View Data Sheet
Name :
GLUL HumanDescription:
Glutamine Synthetase Human Recombinant
GLNS, EC 6.3.1.2, EC 4.1.1.15, GLUL, Glutamine Synthetase, GS, Glutamate decarboxylase, Glutamate--ammonia ligase, PIG43, PIG59.
Product # :
ENZ-544Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
GLUL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (1-373 a.a.) and having a molecular mass of 44.2 kDa. The GLUL is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GLUL Human solution containing 20mM Tris-HCl pH-8, 5mM DTT, 0.2M NaCl & 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is a major source of energy and that takes part in cell proliferation, inhibition of apoptosis, and cell signaling. GLUL is expressed during early fetal stages, and has a role in maintaining body pH by removing ammonia from circulation. Mutations in GLUL gene are related with congenital glutamine deficiency.
-
Synonyms
GLNS, EC 6.3.1.2, EC 4.1.1.15, GLUL, Glutamine Synthetase, GS, Glutamate decarboxylase, Glutamate--ammonia ligase, PIG43, PIG59.
-
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 MTTSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE PKCVEELPEW NFDGSSTLQS EGSNSDMYLV PAAMFRDPFR KDPNKLVLCE VFKYNRRPAE TNLRHTCKRI MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADRA YGRDIVEAHY RACLYAGVKI AGTNAEVMPA QWEFQIGPCE GISMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA GCHTNFSTKA MREENGLKYI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL TGFHETSNIN DFSAGVANRS ASIRIPRTVG QEKKGYFEDR RPSANCDPFS VTEALIRTCL LNETGDEPFQ YKN.
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.
- View Data Sheet
Name :
GCK HumanDescription:
Glucokinase/Hexokinase-4 Human Recombinant
Glucokinase, EC 2.7.1.2, Hexokinase-4, Hexokinase type IV, HK IV, HK4, Hexokinase-D, GCK, GK, GLK, HHF3, HKIV, HXKP, MODY2.
Product # :
PKA-236Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
Glucokinase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 1-465) fused to a 20aa His tag at the N-terminal encoding the sequence of 485 amino acids and having a molecular mass of 54.3 kDa.HK4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (1mg/ml) contains 20mM Tris-HCl pH-8.0 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Alternative splicing of Glucokinase results in three tissue-specific forms of glucokinase, one found in pancreatic islet beta cells and two found in liver. The protein localizes to the outer membrane of mitochondria. In contrast to other forms of hexokinase, HK4 is not inhibited by its product glucose-6-phosphate but remains active while glucose is abundant. Mutations in this gene have been associated with non-insulin dependent diabetes mellitus (NIDDM), maturity onset diabetes of the young, type 2 (MODY2) and persistent hyperinsulinemic hypoglycemia of infancy (PHHI).
-
Synonyms
Glucokinase, EC 2.7.1.2, Hexokinase-4, Hexokinase type IV, HK IV, HK4, Hexokinase-D, GCK, GK, GLK, HHF3, HKIV, HXKP, MODY2.
-
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). Please avoid freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLDDRARMEA AKKEKVEQIL AEFQLQEEDL KKVMRRMQKE MDRGLRLETH EEASVKMLPT YVRSTPEGSE VGDFLSLDLG GTNFRVMLVK VGEGEEGQWS VKTKHQMYSI PEDAMTGTAE MLFDYISECI SDFLDKHQMK HKKLPLGFTF SFPVRHEDID KGILLNWTKG FKASGAEGNN VVGLLRDAIK RRGDFEMDVV AMVNDTVATM ISCYYEDHQC EVGMIVGTGC NACYMEEMQN VELVEGDEGR MCVNTEWGAF GDSGELDEFL LEYDRLVDES SANPGQQLYE KLIGGKYMGE LVRLVLLRLV DENLLFHGEA SEQLRTRGAF ETRFVSQVES DTGDRKQIYN ILSTLGLRPS TTDCDIVRRA CESVSTRAAH MCSAGLAGVI NRMRESRSED VMRITVGVDG SVYKLHPSFK ERFHASVRRL TPSCEITFIE SEEGSGRGAA LVSAVACKKA CMLGQ.
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.
- View Data Sheet
Name :
REG1A HumanDescription:
Regenerating Islet-Derived 1 Alpha Human Recombinant
Lithostathine-1-alpha, Pancreatic stone protein, PSP, Pancreatic thread protein, PTP, Islet of Langerhans regenerating protein, REG, Regenerating protein I alpha, Islet cells regeneration factor, ICRF, REG1A, PSPS, P19, PSPS1, MGC12447.
Product # :
PRO-289Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
The Recombinant Human REG 1 alpha is produced with N-terminal fusion His Tag. The Recombinant Human REG 1 alpha His-Tagged Fusion Protein, has a molecular weight of 17.8 kDa protein containing 144 amino acid residues of the Human REG 1 alpha and 12 additional amino acid residues – His Tag.
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 5mM Tris, 25mM NaCl, pH 7.5.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
REG protein was shown to be stimulated during the regeneration of pancreatic islets. Since then, many Reg-related proteins have been identified in humans and other animals. In human, the four REG family genes, i.e., REG 1 alpha, REG 1 beta, REG-related sequence (RS) and HIP/PAP, have so far been isolated. These Reg-related proteins are classified into four subfamilies according to their amino-acid sequences, but they share a similar structure and physiological function. Reg protein is a growth factor for pancreatic beta cells and also suggests that the administration of Reg protein could be used as another therapeutic approach for diabetes mellitus. Human REG cDNA which encodes a 166-amino acid protein with a 22-amino acid signal peptide. The amino acid sequence of human REG protein has 68% homology to that of rat Reg protein.
Reg I was found to be expressed mainly in pancreatic beta and acinoductular cells as well as gastric fundic enterochromaffin-like (ECL) cells. Reg I production in ECL cells is stimulated by gastrin, as well as by the proinflammatory cytokine, cytokine-induced neutrophil chemoattractant (CINC)-2Beta. In patients with chronic hypergastrinemia, Reg production is stimulated, with the increased proliferation of gastric mucosal cells. Patients with Helicobacter pylori infection also showed increased Reg production in the gastric mucosa, partly via increased plasma gastrin concentration and partly via increased proinflammatory cytokine production. The serum concentration of the reg-protein was significantly higher in patients with various pancreatic diseases than in normal controls, and was also significantly higher in patients with acute pancreatitis or chronic relapsing pancreatitis than in patients with chronic pancreatitis. Furthermore, the serum PSP/reg-protein concentration was also significantly increased in liver cirrhosis, choledocholithiasis, and various cancers of the digestive system. -
Synonyms
Lithostathine-1-alpha, Pancreatic stone protein, PSP, Pancreatic thread protein, PTP, Islet of Langerhans regenerating protein, REG, Regenerating protein I alpha, Islet cells regeneration factor, ICRF, REG1A, PSPS, P19, PSPS1, MGC12447.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
Add deionized water to a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
MKHHHHHHAS HMQEAQTELP QARISCPEGT NAYRSYCYYF NEDRETWVDA DLYCQNMNSG NLVSVLTQAE GAFVASLIKE SGTDDFNVWI GLHDPKKNRR WHWSSGSLVS YKSWGIGAPS SVNPGYCVSL TSSTGFQKWK DVPCEDKFSF VCKFKN.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin tA Rat, PEGDescription:
Leptin Antagonist Triple Mutant Pegylated Rat Recombinant
Product # :
CYT-567Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Leptin Antagonist Triple Mutant Rat Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa.The Rat Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant.The Rat Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Rat Leptin triple anatagonist runs as a 48 kDa.Leptin Antagonist Triple Mutant Rat Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Rat Leptin triple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Leptin Antagonist Triple Mutant Rat Recombinant half-life in circulation after SC injection was over 20 hours.
Leptin Antagonist Triple Mutant Rat Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Leptin Antagonist Triple Mutant Rat Recombinant in vitro activity is 5-6 fold lower than the non-pegylated antagonist, though in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake.Citations
More Info
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leptin Antagonist Triple Mutant Rat Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP mutant can be stored at 4°C 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 Leptin Antagonist Triple Mutant Rat Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
-
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Globular Adiponectin MouseDescription:
Globular Adiponectin Mouse Recombinant
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-432Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- sds-page
- Citations
Description
The globular domain of Adiponectin Mouse Recombinant / Acrp30 Mouse contains 138 amino acid residues from a.a. 111-247 having molecular mass of 16 kDa was over expressed in E.coli and purified by using conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
Acrp30 Mouse (1mg/ml) solution containing 20mM Tris-HCl pH7.5, 50mM NaCl, 5mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
Citations
More Info
-
Introduction
Adiponectin (247amino acids) is adipocyte complement-related protein of 30 kDa and exclusively expressed in differentiated adipocytes. APM-1 (Acrp30 Mouse) is a member of the complement factor C1q family and consists of signal sequence, Non-homologous sequence, collagen domain and domain (gAcrp30).
Adiponectin expression is reduced in a variety of obese and insulin-resistant states in human, monkeys and mice. Injection of Acrp30 Mouse (247aa) or gAcrp30 (globular domain) lowers serum glucose and free fatty acid level in mice. -
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
-
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
MAYMYRSAFS VGLETRVTVP NVPIRFTKIF YNQQNHYDGS TGKFYCNIPG LYYFSYHITVYMKDVKVSLF KKDKAVLFTY DQYQEKNVDQ ASGSVLLHLE VGDQVWLQVY GDGDHNGLYADNVNDSTFTG FLLYHDTN
-
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 16kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% 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?
MAYMYRSAFS VGLETRVTVP NVPIRFTKIF YNQQNHYDGS TGKFYCNIPG LYYFSYHITVYMKDVKVSLF KKDKAVLFTY DQYQEKNVDQ ASGSVLLHLE VGDQVWLQVY GDGDHNGLYADNVNDSTFTG FLLYHDTN
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.
- View Data Sheet
Name :
GAD2 HumanDescription:
Glutamate Decarboxylase 2 Human Recombinant
Glutamate Decarboxylase 2 (Pancreatic Islets And Brain, 65kDa), Glutamate Decarboxylase 65 KDa Isoform, 65 KDa Glutamic Acid Decarboxylase, EC 4.1.1.15, GAD-65, GAD65, Glutamate Decarboxylase 2 (Pancreatic Islets And Brain, 65kD), Glutamate Decarboxylase-2 (Pancreas), EC 4.1.1, GAD2.
Product # :
ENZ-937Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
Recombinant Human GAD2 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 61 kDa. GAD2 is expressed with a 6xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
GAD2 protein solution is supplied in 20mM Sodium phosphate pH-7.4, 150mM NaCl, 0.016mM Pyridoxal-5’-Phosphate, 0.05% Tergitol 15-S-9 and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Glutamate Decarboxylase 2 (GAD2) is one of several forms of glutamic acid decarboxylase, identified as a main autoantigen in type II diabetes. The GAD2 enzyme is responsible for catalyzing the production of gamma-aminobutyric acid from L-glutamic acid. A pathogenic role for the GAD2 enzyme has been characterized in the human pancreas since it has been identified as an autoantibody and an autoreactive T cell target in type II diabetes. GAD2 gene may also have a role in the stiff man syndrome. In addition, GAD2 catalyzes the production of GABA.
-
Synonyms
Glutamate Decarboxylase 2 (Pancreatic Islets And Brain, 65kDa), Glutamate Decarboxylase 65 KDa Isoform, 65 KDa Glutamic Acid Decarboxylase, EC 4.1.1.15, GAD-65, GAD65, Glutamate Decarboxylase 2 (Pancreatic Islets And Brain, 65kD), Glutamate Decarboxylase-2 (Pancreas), EC 4.1.1, GAD2.
-
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. Avoid multiple freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.