Search: 1000 results found for "Prothymosin"

Description:

Myostatin Human Recombinant, HEK

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

Product # :

CYT-833

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

Myostatin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn24-Ser375) containing a total of 360 amino acids, having a calculated molecular mass of 41.1kDa. Myostatin is fused to a 2 aa N-terminal linker and a 6 aa His tag at N-Terminus.

Source

HEK 293.

Formulation

Myostatin solution at a concentration of 0.25mg/ml in phosphate buffered saline (PBS) pH 8.0 and 20% (w/v) glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.
Synonyms
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
Physical Appearance
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
HHHHHHASNE NSEQKENVEK EGLCNACTWR QNTKSSRIEA IKIQILSKLR LETAPNISKD VIRQLLPKAP PLRELIDQYD VQRDDSSDGS LEDDDYHATT ETIITMPTES DFLMQVDGKP KCCFFKFSSK IQYNKVVKAQ LWIYLRPVET PTTVFVQILR LIKPMKDGTR YTGIRSLKLD MNPGTGIWQS IDVKTVLQNW LKQPESNLGI EIKALDENGH DLAVTFPGPG EDGLNPFLEV KVTDTPKRSR RDFGLDCDEH STESRCCRYP LTVDFEAFGW DWIIAPKRYK ANYCSGECEF VFLQKYPHTH LVHQANPRGS AGPCCTPTKM SPINMLYFNG KEQIIYGKIP AMVVDRCGCS.

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:

Proteasome Subunit Beta Type 1 Human Recombinant

HC5, PSC5, PMSB1, FLJ25321, KIAA1838, PSMB1, Proteasome subunit beta type-1, Proteasome component C5, Macropain subunit C5, Multicatalytic endopeptidase complex subunit C5, Proteasome gamma chain.

Product # :

ENZ-405

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

PSMB1 Human Recombinant fused to a 37 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 250 amino acids (30-241) and having a molecular mass of 27.7 kDa. The PSMB1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PSMB1 solution contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
PSMB1 is part of the proteasome B-type family, also identified as the T1B family, that is a 20S core beta subunit. PSMB1 is tightly linked to the TBP (TATA-binding protein) gene in human and in mouse, and is transcribed in the opposite orientation in both species.The main function of PSMB1 is its degradation activity of unnecessary or damaged proteins by proteolysis. PSMB1 is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with arg, phe, tyr, leu, and glu adjacent to the leaving group at neutral or slightly basic ph. the proteasome has an atp-dependent proteolytic activity.
Synonyms
HC5, PSC5, PMSB1, FLJ25321, KIAA1838, PSMB1, Proteasome subunit beta type-1, Proteasome component C5, Macropain subunit C5, Multicatalytic endopeptidase complex subunit C5, Proteasome gamma chain.
Physical Appearance
Sterile Filtered clear 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 KDRWGSHMFS PYVFNGGTIL AIAGEDFAIV ASDTRLSEGF SIHTRDSPKC YKLTDKTVIG CSGFHGDCLT LTKIIEARLK MYKHSNNKAM TTGAIAAMLS TILYSRRFFP YYVYNIIGGL DEEGKGAVYS FDPVGSYQRD SFKAGGSASA MLQPLLDNQV GFKNMQNVEH VPLSLDRAMR LVKDVFISAA ERDVYTGDAL RICIVTKEGI REETVSLRKD.

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:

Proteasome Activator Subunit 2 Human Recombinant

Proteasome (prosome, macropain) activator subunit 2 (PA28 beta), PA28beta, Activator of multicatalytic protease subunit 2, Proteasome activator 28 subunit beta, 11S regulator complex subunit beta, PA28B, REG-beta, cell migration-inducing protein 22, MCP activator 31-kD subunit, proteasome activator complex subunit 2, Proteasome activator hPA28 subunit beta.

Product # :

PRO-975

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

PSME2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 259 amino acids (1-239) and having a molecular mass of 29.5 kDa.PSME2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The PSME2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT, 0.1mM PMSF and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
PSME2 is an IFN-gamma inducible proteasome activator essential for production of several key histocompatibility (MHC) class I antigens. Downregulation of PSME2 causes unusual proteasome activation and is connected to the development of intimal hyperplasia (IH) in animal models.
Synonyms
Proteasome (prosome, macropain) activator subunit 2 (PA28 beta), PA28beta, Activator of multicatalytic protease subunit 2, Proteasome activator 28 subunit beta, 11S regulator complex subunit beta, PA28B, REG-beta, cell migration-inducing protein 22, MCP activator 31-kD subunit, proteasome activator complex subunit 2, Proteasome activator hPA28 subunit beta.
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 MAKPCGVRLS GEARKQVEVF RQNLFQEAEE FLYRFLPQKI IYLNQLLQED SLNVADLTSL RAPLDIPIPD PPPKDDEMET DKQEKKEVPK CGFLPGNEKV LSLLALVKPE VWTLKEKCIL VITWIQHLIP KIEDGNDFGV AIQEKVLERV NAVKTKVEAF QTTISKYFSE RGDAVAKASK ETHVMDYRAL VHERDEAAYG ELRAMVLDLR AFYAELYHII SSNLEKIVNP KGEEKPSMY

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 Human Recombinant, His Tag

Procalcitonin, PCT.

Product # :

HOR-295

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

Procalcitonin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 114 amino acids fragment (3-116) having a molecular mass of 17.13 kDa and an amino-terminal hexahistidine tag. The PCT is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

PCT is supplied in 20mM Tris-HCl pH 8.0 and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

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
Procalcitonin, PCT.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please prevent freeze-thaw cycles.
Background
What is the molecular weight/Mw of PROCALCITONIN HUMAN, HIS Protein?
PROCALCITONIN HUMAN, HIS Protein has a total Mw of 17.13kDa.

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

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

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

What is the amino acid sequence of PROCALCITONIN HUMAN, HIS Protein?
PROCALCITONIN HUMAN, HIS Protein is composed from 114 amino acids.

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

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

Who supplies recombinant PROCALCITONIN HUMAN, HIS 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 HUMAN, HIS?
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:

Orosomucoid 1 Human Recombinant

Orosomucoid 1, ORM, AGP1, OMD 1, AGP-A, alpha-1-acid glycoprotein 1.

Product # :

PRO-889

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

ORM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 184 amino acids (19-201) and having a molecular mass of 21.7 kDa.The ORM1 is purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ORM1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 5% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
The acute phase plasma protein ORM1 synthesized by the liver mediates the interaction between blood cells and endothelial cells. In addition, together with haptoglobin and C reactive protein, ORM1 regulates the extravasation of the cells through infection and inflammation. Expression of ORM1 is induced by acute-phase stimulatory mediators such as bacterial lipopolysaccharides.
Synonyms
Orosomucoid 1, ORM, AGP1, OMD 1, AGP-A, alpha-1-acid glycoprotein 1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MQIPLCANLV PVPITNATLD QITGKWFYIA SAFRNEEYNK SVQEIQATFF YFTPNKTEDT IFLREYQTRQ DQCIYNTTYL NVQRENGTIS RYVGGQEHFA HLLILRDTKT YMLAFDVNDE KNWGLSVYAD KPETTKEQLG EFYEALDCLR IPKSDVVYTD WKKDKCEPLE KQHEKERKQE EGES.

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:

Pleiotrophin Human Recombinant, His Tag

PTN, Heparin Affin Regulatory Protein, HARP, Heparin-binding growth factor-8, HBGF-8, Osteoblast-Specific Factor-1, OSF-1, Heparin-binding growth-associated molecule, HB-GAM, HBNF-1 Heparin-binding brain mitogen, Heparin-binding neurite outgrowth-promoting factor 1, HBBM, NEGF1.

Product # :

CYT-451

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

Pleiotrophin Human Recombinant contains His-Tagged Fusion Protein, produced in E. coli, its molecular weight is 17.3 kDa protein containing 136 amino acid residues of the OSF-1 human and 16 additional amino acid residues - HisTag, thrombin cleavage site (underlined).

Source

Escherichia Coli.

Formulation

Filtered and lyophilized from 0.5 mg/ml in 0.1M phosphate buffer and 0.1M NaCl, pH 7.2.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Pleiotrophin (Osteoblast-Specific Factor-1, OSF-1) contains 136 amino acid residues. The sequence is very rich in cationic amino acids (24% of the residues); lysine cluster sequences are found in the N-terminal and C-terminal ends of the structure.
The OSF-1 gene was shown by Northern blotting analysis to be expressed in mouse calvarial osteoblast-enriched cells and in mouse brain tissues, but not in thymus, spleen, kidney, liver, lung, testis or heart. Pleiotrophin has the ability to promote adhesion, migration, expansion, and differentiation of human osteoprogenitor cells. In addition to certain types of cancer, the embryonic growth and differentiation factor pleiotrophin is found also in adults in inflammatory diseases. In osteoarthritis, pleiotrophin is especially expressed in early stages, and its concentrations in the synovial fluid could serve as a marker for the progress of the disease. Pleitrophin might be involved in cartilage repair in osteoarthritis, in particular, in earlier stages.
Synonyms
PTN, Heparin Affin Regulatory Protein, HARP, Heparin-binding growth factor-8, HBGF-8, Osteoblast-Specific Factor-1, OSF-1, Heparin-binding growth-associated molecule, HB-GAM, HBNF-1 Heparin-binding brain mitogen, Heparin-binding neurite outgrowth-promoting factor 1, HBBM, NEGF1.
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
Add PBS pH 7.2 and let the lyophilized pellet dissolve completely.
Amino Acid Sequence
MKHHHHHHHM LVPRGSGKKE KPEKKVKKSD CGEWQWSVCV PTSGDCGLGT REGTRTGAEC KQTMKTQRCK IPCNWKKQFG AECKYQFQAW GECDLNTALK TRTGSLKRAL HNAECQKTVT ISKPCGKLTK PKPQAESKKK KKEGKKQEKM LD.

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:

Calmodulin Bovine

Calmodulin, CaM, CALM.

Product # :

PRO-2800

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

source
formulation
purity
More Info
Citations

Source

Bovine brain tissue.

Formulation

CALM was lyophilized with 2mM EDTA.

Purity

Greater than 95.0%.

More Info

Synonyms
Calmodulin, CaM, CALM.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CALM although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Calmodulin 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 CALM in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Applications
Biochemical and immunochemical investigations.
Background
Role in Muscle Contraction and Relaxation:
In muscle cells, calmodulin plays a pivotal role in the regulation of contraction and relaxation. It interacts with myosin light-chain kinase during muscle contraction, initiating the process of cross-bridge cycling. Conversely, during muscle relaxation, calmodulin activates the enzyme myosin light-chain phosphatase, leading to the dephosphorylation of myosin and muscle relaxation. This delicate balance is crucial for proper muscle function.
Neuronal Signalling and Synaptic Plasticity:
In neurons, calmodulin is essential for neurotransmitter release and synaptic plasticity. It modulates the activity of proteins involved in vesicle fusion and neurotransmitter release. Additionally, calmodulin-dependent protein kinases (CaMKs) are critical for synaptic plasticity, learning, and memory. The intricate interplay between calmodulin and neuronal proteins underpins the fundamental processes of learning and cognition.
Implications in Disease and Therapeutics:
Dysregulation of calmodulin has been implicated in various diseases, including cardiac arrhythmias and neurodegenerative disorders. Mutations in calmodulin genes can lead to aberrant calcium signalling and cellular dysfunction. Consequently, understanding these molecular mechanisms offers potential therapeutic targets. Researchers are exploring calmodulin inhibitors and modulators for conditions like cardiac arrhythmias, aiming to restore normal cellular function.
Conclusion:
Calmodulin, with its remarkable structural versatility and central role in cellular signalling, epitomizes the complexity of biological regulation. Its influence spans from the fundamental processes of muscle contraction to the intricacies of neuronal signalling. Unravelling the mysteries of calmodulin not only deepens our understanding of basic biological phenomena but also holds the promise of innovative therapeutic interventions. This research illuminates calmodulin's significance, emphasizing its position as a master regulator in the orchestra of cellular life.

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:

Macrophage Inflammatory protein-4 (CCL18) Human Recombinant, His-Tag

Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.

Product # :

CHM-339

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
SDS-PAGE
Citations

Description

MIP-4 Human Recombinant fused with a 25 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 93 amino acids (22-89 a.a.) and having a molecular mass of 10.4kDa. The MIP-4 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MIP-4 solution (0.25 mg/ml) contains 10mM Sodium Citrate pH3.5 and 10% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
Chemokine (C-C motif) ligand 18 (CCL18) is a small cytokine belonging to the CC chemokine family that was previously called PARC (pulmonary and activation-regulated chemokine). CCL18 is approximately 60% identical in amino acid sequence to CCL3. It is expressed at high levels in lung and at lower levels in certain lymphoid tissues, such as the lymph nodes, and is chemotactic for activated T cells and non activated lymphocytes. The gene for human CCL18 contains three exons and is located on chromosome 17.
Synonyms
Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.
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 MGSHMQVGTN KELCCLVYTS WQIPQKFIVD YSETSPQCPK PGVILLTKRG RQICADPNKK WVQKYISDLK LNA.
Background
What is the molecular weight/Mw of CCL18 HUMAN, HIS Protein?
CCL18 HUMAN, HIS Protein has a total Mw of 10.4kDa.

What is the source or expression system of CCL18 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of CCL18 HUMAN, HIS Protein?
CCL18 HUMAN, HIS Protein is > 95% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL18 HUMAN, HIS Protein?
The biological functionality of CCL18 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of CCL18 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMQVGTN KELCCLVYTS WQIPQKFIVD YSETSPQCPK PGVILLTKRG RQICADPNKK WVQKYISDLK LNA.

What applications can CCL18 HUMAN, HIS Protein be used in?
CCL18 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL18 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL18 HUMAN, HIS Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL18 HUMAN, HIS 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 CCL18 HUMAN, HIS?
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:

Ovine Prolactin Recombinant, His Tag

Mammotropin, Luteotropic hormone, Luteotropin, PRL.

Product # :

CYT-1185

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

Prolactin Ovine produced in E.Coli is a single, non-glycosylated polypeptide chain, fused to a 6 His Tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

(1mg/ml) in 1 X PBS, pH 7.2 and 50% glycerol.

Purity

Protein is >90% pure as determined by SDS-PAGE.

More Info

Introduction
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Prolactin’s primary function is to promote and maintain lactation and also in breast cancer development, regulation of reproductive function and immunoregulation.
Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
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.

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:

Proteasome Subunit Beta Type 5 Human Recombinant

Proteasome subunit beta type-5, Macropain epsilon chain, Multicatalytic endopeptidase complex epsilon chain, Proteasome chain 6, Proteasome epsilon chain, Proteasome subunit MB1, Proteasome subunit X, PSMB5, LMPX, MB1, X, MGC104214.

Product # :

ENZ-050

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

PSMB5 Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 241 amino acids (60-263 a.a.) and having a molecular mass of 26.7kDa. The PSMB5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PSMB5 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 5mM DTT and 0.2M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
PSMB5 belongs to the proteasome B-type family that has a 20S core beta subunit in the proteasome. This catalytic subunit is not present in the immunoproteasome and is substituted by catalytic subunit 3i (proteasome beta 8 subunit). A fundamental function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. PSMB5 exhibits an ATP dependent proteolytic activity and is involved in an ATP/ubiquitin dependent non lysosomal proteolytic pathway.
Synonyms
Proteasome subunit beta type-5, Macropain epsilon chain, Multicatalytic endopeptidase complex epsilon chain, Proteasome chain 6, Proteasome epsilon chain, Proteasome subunit MB1, Proteasome subunit X, PSMB5, LMPX, MB1, X, MGC104214.
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 KDRWGSMTTT LAFKFRHGVI VAADSRATAG AYIASQTVKK VIEINPYLLG TMAGGAADCS FWERLLARQC RIYELRNKER ISVAAASKLL ANMVYQYKGM GLSMGTMICG WDKRGPGLYY VDSEGNRISG ATFSVGSGSV YAYGVMDRGY SYDLEVEQAY DLARRAIYQA TYRDAYSGGA VNLYHVREDG WIRVSSDNVA DLHEKYSGST 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:

Thrombopoietin Mouse Recombinant, HEK

Thpo, C-mpl ligand,ML, Megakaryocyte colony-stimulating factor, Megakaryocyte growth and development factor, MGDF, Myeloproliferative leukemia virus oncogene ligand, Mgdf, Ml, Mpllg, Tpo, thrombopoietin isoform 1.

Product # :

CYT-1157

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

TPO Mouse Recombinant produced in HEK293 cells is a single, non-glycosylated polypeptide chain containing 341 amino acids ( 22-356 a.a) and having a molecular mass of 36.4kDa. TPO is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293.

Formulation

TPO protein (0.5mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Measured in a cell proliferation assay using MO7e human megakaryocytic leukemic cells. The ED50 range ≤4ng/ml.

Biological Activity

Measured by its ability to agglutinate human red blood cells. The ED50 for this effect is ≥ 25ug/ml.

More Info

Introduction
Thrombopoietin or TPO or MGDF, is a protein (glycoprotein hormone) that can be found in the liver and kidney tissues. TPO regulates the creation of platelets. The protein enhances the production & differentiation of cells such as megakaryocytes that are part of the bone marrow cells that secretes a wide number of platelets. The cellular development process that ends up in the production of platelet calls (Megakaryocytopoiesis). Humoral growth factor is needed for the megakaryocyte proliferation & maturation of megakaryocyte, not apart from thrombopoiesis.
Synonyms
Thpo, C-mpl ligand,ML, Megakaryocyte colony-stimulating factor, Megakaryocyte growth and development factor, MGDF, Myeloproliferative leukemia virus oncogene ligand, Mgdf, Ml, Mpllg, Tpo, thrombopoietin isoform 1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
SPVAPACDPR LLNKLLRDSH LLHSRLSQCP DVDPLSIPVL LPAVDFSLGE WKTQTEQSKA QDILGAVSLL LEGVMAARGQ LEPSCLSSLL GQLSGQVRLL LGALQGLLGT QLPLQGRTTA HKDPNALFLS LQQLLRGKVR FLLLVEGPTL CVRRTLPTTA VPSSTSQLLT LNKFPNRTSG LLETNFSVTA RTAGPGLLSR LQGFRVKITP GQLNQTSRSP VQISGYLNRT HGPVNGTHGL FAGTSLQTLE ASDISPGAFN KGSLAFNLQG GLPPSPSLAP DGHTPFPPSP ALPTTHGSPP QLHPLFPDPS TTMPNSTAPH PVTMYPHPRN LSQETHHHHH H.

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:

Proteasome Subunit Alpha Type 8 Human Recombinant

Proteasome subunit alpha type-7-like, PSMA8, PSMA7L.

Product # :

ENZ-203

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

PSMA8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 270 amino acids (1-250) and having a molecular mass of 30kDa.PSMA8 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The PSMA8 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
Proteasome subunit alpha type-8 (PSMA8) is a member of the peptidase T1A family. PSMA8 is a multicatalytic proteinase complex which is distinguished by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. The PSMA8 subunit may be testis-specific.
Synonyms
Proteasome subunit alpha type-7-like, PSMA8, PSMA7L.
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 MASRYDRAIT VFSPDGHLFQ VEYAQEAVKK GSTAVGIRGT NIVVLGVEKK SVAKLQDERT VRKICALDDH VCMAFAGLTA DARVVINRAR VECQSHKLTV EDPVTVEYIT RFIATLKQKY TQSNGRRPFG ISALIVGFDD DGISRLYQTD PSGTYHAWKA
NAIGRSAKTV REFLEKNYTE DAIASDSEAI KLAIKALLEV VQSGGKNIEL AIIRRNQPLK MFSAKEVELY VTEIEKEKEE AEKKKSKKSV.

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:

Monocyte Chemotactic Protein-1 Mouse Recombinant (CCL2), His Tag

Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.

Product # :

CHM-014

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
SDS-PAGE
Citations

Description

MCP-1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 146 amino acids (24-148 a.a) and having a molecular mass of 16kDa.MCP-1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MCP-1 protein solution (0.25mg/ml) containing PBS (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belonging to the CC chemokine family that is also known as monocyte chemotactic protein-1 (MCP-1). It is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts and osteoblasts and is under the control of nuclear factor ?B (NF?B). CCL2 recruits immune cells, such as monocytes, to sites of tissue injury and infection. This chemokine is produced as a protein precursor containing signal peptide of 23 amino acids and a mature peptide of 76 amino acids. It is a monomeric polypeptide, with a molecular weight of approximately 13kDa. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans. The cell surface receptors that bind CCL2 are CCR2 and CCR5.
Synonyms
Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.
Physical Appearance
Sterile Filtered colorless 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 MQPDAVNAPL TCCYSFTSKM IPMSRLESYK RITSSRCPKE AVVFVTKLKR EVCADPKKEW VQTYIKNLDR NQMRSEPTTL FKTASALRSS APLNVKLTRK SEANASTTFS TTTSSTSVGV TSVTVN.
Background
What is the molecular weight/Mw of CCL2 MOUSE, HIS Protein?
CCL2 MOUSE, HIS Protein has a total Mw of 16kDa.

What is the source or expression system of CCL2 MOUSE, HIS Protein?
Escherichia Coli.

What is the Purity of CCL2 MOUSE, HIS Protein?
CCL2 MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL2 MOUSE, HIS Protein?
The biological functionality of CCL2 MOUSE, HIS Protein will be determined in the future.

What is the amino acid sequence of CCL2 MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MQPDAVNAPL TCCYSFTSKM IPMSRLESYK RITSSRCPKE AVVFVTKLKR EVCADPKKEW VQTYIKNLDR NQMRSEPTTL FKTASALRSS APLNVKLTRK SEANASTTFS TTTSSTSVGV TSVTVN.

What applications can CCL2 MOUSE, HIS Protein be used in?
CCL2 MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL2 MOUSE, HIS Protein?
The endotoxin level is minimal, CCL2 MOUSE, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL2 MOUSE, HIS 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 CCL2 MOUSE, HIS?
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:

Leptin Pufferfish Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-530

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Leptin Pufferfish (Takifugu rubripes) Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 16 kDa. Bioactive Leptin Pufferfish (Takifugu rubripes) Recombinant was prepared according to the sequence published by Kurokawa et al. (2005)Peptides 26, 745-750 in two forms: monomer and covalent dimer. MS analysis revealed molecular masses of 15,291 and 30,585 Da, close to the theoretical values of 15,270 and 30,540 Da. CD spectra revealed high similarity to mammalian leptins. Other details of its preparation will be soon published by Yacobovitz et al (in press), General and Comparative Endocrinology.The Pufferfish Leptin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Pufferfish Leptin was lyophilized from a concentrated (0.85mg/ml) solution with 0.003mM NaHCO3.

Purity

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

Biological Activity

Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. The affinity of human leptin receptors is considerably lower campared to mammalian leptins.

More Info

Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Pufferfish Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Pufferfish Leptin in sterile 0.4% NaHCO3 pH-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ALPGALDAMDVEKMKSKVTWKAQGLVARIDKHFPDRGLRFDTDKVE
GSTSVVASLESYNNLISDRFGGVSQIKTEISSLAGYLNHWREGNCQE
QQPKVWPRRNIFNHTVSLEALMRVREFLKLLQKNVDLLERC
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.28 as the extinction coefficient for a 0.1% (1mg/ml) solution. 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.

Description:

Oncomodulin-1 Human Recombinant

Oncomodulin-1, OM, Parvalbumin beta, OCM, OCM1, OCMN.

Product # :

PRO-143

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
More Info
Citations

Description

The Recombinant Human Oncomodulin-1 produced in E.coli has a molecular mass of 13.21kDa containing 117 amino acid residues of the human Oncomodulin-1 and fused to a 9 a.a. His tag at N-terminus.

Source

Escherichia Coli.

Formulation

Oncomodulin-1 was filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.

More Info

Introduction
Oncomodulin is a member of the superfamily of calmodulin proteins, otherwise known as the EF-hand proteins. It is a high-affinity calcium ion-binding protein. Oncomodulin is an oncodevelopmental protein which is found in early embryonic cells in the placenta and also in tumors.
Synonyms
Oncomodulin-1, OM, Parvalbumin beta, OCM, OCM1, OCMN.
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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHAS ITDVLSADDI S ITDVLSADDI AAALQECRDP DTFEPQKFFQ TSGLSKMSAN QVKDVFRFID NDQSGYLDEE ELKFFLQKFE SGARELTESE TKSLMAAADN DGDGKIGAEE FQEMVHS.
Applications
Western blotting.

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:

Omentin Human Recombinant, His Tag

Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

Product # :

CYT-551

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info
Citations

Description

Omentin Human Recombinant is produced in E.Coli by recombinant DNA technology is a single, polypeptide chain containing 294 amino acids and having a molecular mass of 32.7 kDa. Recombinant Human Omentin contains His tag fused at N-Terminus.Intelectin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Each mg of lyophilized powder contains 20mM Tris & 50mM NaCl pH-8.0.

Purity

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

More Info

Introduction
Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase insulin-stimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of insulin presence. Its role in glucose metabolism and obesity remains to be described; an insulin-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.
Synonyms
Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Intelectin His Tag although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Intelectin 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 Omentin His Tag in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MRGSHHHHHH GMASTDEANT YFKEWTCSSS PSLPRSCKEI KDECPSAFDG LYFLRTENGV IYQTFCDMTS GGGGWTLVAS VHENDMRGKC TVGDRWSSQQ GSKAVYPEGD GNWANYNTFG SAEAATSDDY KNPGYYDIQA KDLGIWHVPN KSPMQHWRNS SLLRYRTDTG FLQTLGHNLF GIYQKYPVKY GEGKCWTDNG PVIPVVYDFG DAQKTASYYS PYGQREFTAG FVQFRVFNNE RAANALCAGM RVTGCNTEHH CIGGGGYFPE ASPQQCGDFS GFDWSGYGTH VGYS.
Applications
Elisa
Western blot.

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:

Otoraplin Human Recombinant, His Tag

Otoraplin, Melanoma Inhibitory Activity-Like Protein, Fibrocyte-Derived Protein, FDP, MIAL1, MIAL, Melanoma inhibitory activity-like protein.

Product # :

CYT-884

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

OTOR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (26-128 a.a) and having a molecular mass of 14.3kDa. OTOR is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

OTOR protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
OTOR proteins is also known as fibrocyte-derived protein (Fdp) and Melanoma inhibitory activity-like (MIAL). Otoraplin is a member of the melanoma-inhibiting activity gene family. Otoraplin is a secreted 16 kDa globular protein that is expressed in the inner ear by periotic mesenchyme and developing and mature fibrocytes. OTOR is highly homologous to MIA/cartilage-derived retinoic acid-sensitive protein (CD-RAP), which is a cartilage-specific protein that is also expressed in malignant melanoma cells. The 111 amino acid mature human otoraplin contains 1 SH3 domain (46 – 107 amino acids) and a Tyr at position 50 that is reportedly sulfated. Otoraplin takes pasrt in the initiation of periotic mesenchyme chondrogenesis.
Otoraplin is secreted through the Golgi apparatus and plays a role in cartilage development and maintenance. A frequent polymorphism in the translation start codon of OTOR can abolish translation and may be associated with forms of deafness.
Synonyms
Otoraplin, Melanoma Inhibitory Activity-Like Protein, Fibrocyte-Derived Protein, FDP, MIAL1, MIAL, Melanoma inhibitory activity-like protein.
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).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMLASKK LCADDECVYT ISLASAQEDY NAPDCRFINV KKGQQIYVYS KLVKENGAGE FWAGSVYGDG QDEMGVVGYF PRNLVKEQRV YQEATKEVPT TDIDFFCE.

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:

Proteasome Assembly Chaperone 2 Human Recombinant

Proteasome assembly chaperone 2, PAC-2, Hepatocellular carcinoma-susceptibility protein 3, Tumor necrosis factor superfamily member 5-induced protein 1, PSMG2, HCCA3, PAC2, TNFSF5IP1, CLAST3, MDS003, HsT1707, MGC15092.

Product # :

PRO-930

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
Citations

Description

PSMG2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 287 amino acids (1-264 a.a.) and having a molecular mass of 31.8kDa.PSMG2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PSMG2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol and 0.1M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Proteasome assembly chaperone 2 (PSMG2) stimulates assembly of the 20S proteasome as part of a heterodimer with PSMG1. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits and promotes compilation of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization. PSMG2 is widely expressed with highest levels in the lung, brain and colon. It is moderately expressed in the muscle, stomach, spleen and heart, and weakly expressed in the small intestine, pancreas and liver. It is also highly expressed in hepatocellular carcinomas with low levels in surrounding liver tissue.
Synonyms
Proteasome assembly chaperone 2, PAC-2, Hepatocellular carcinoma-susceptibility protein 3, Tumor necrosis factor superfamily member 5-induced protein 1, PSMG2, HCCA3, PAC2, TNFSF5IP1, CLAST3, MDS003, HsT1707, MGC15092.
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 MGSMFVPCGE SAPDLAGFTL LMPAVSVGNV GQLAMDLIIS TLNMSKIGYF YTDCLVPMVG NNPYATTEGN STELSINAEV YSLPSRKLVA LQLRSIFIKY KSKPFCEKLL SWVKSSGCAR VIVLSSSHSY QRNDLQLRST PFRYLLTPSM QKSVQNKIKS LNWEEMEKSR CIPEIDDSEF CIRIPGGGIT KTLYDESCSK EIQMAVLLKF VSEGDNIPDA LGLVEYLNEW LQILKPLSDD PTVSASRWKI PSSWRLLFGS GLPPALF.

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:

LL-37

LL37, antibacterial protein LL-37, cathelicidin LL 37, camp.

Product # :

HOR-041

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
formulation
purity
More Info
Citations

Description

LL-37 Synthetic is a single, non-glycosylated polypeptide chain containing 37 amino acids, having a molecular mass of 4493 Dalton and a Molecular formula of C205H340N60O53.

Formulation

The protein was lyophilized with no additives.

Purity

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

More Info

Synonyms
LL37, antibacterial protein LL-37, cathelicidin LL 37, camp.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized LL-37 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LL-37 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 LL-37 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-Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser-OH.
Background
LL-37, a prominent member of the human cathelicidin family, has emerged as a pivotal host defense peptide with diverse biological functions. This research paper aims to provide a comprehensive analysis of LL-37, elucidating its biochemical properties, antimicrobial activity, immunomodulatory effects, and potential therapeutic applications.
LL-37, derived from the precursor protein hCAP18, plays a crucial role in innate immunity and host defense against microbial pathogens. Beyond its well-established antimicrobial properties, LL-37 exhibits various immunomodulatory effects, making it an intriguing target for therapeutic interventions (Lai & Gallo, 2009). This paper aims to delve into the complexities of LL-37, uncovering its multifaceted nature and potential clinical applications.
LL-37 is a cationic peptide characterized by a helical structure that facilitates its interaction with microbial membranes. Its amphipathic nature enables it to penetrate microbial membranes, leading to disruption and subsequent cell death (Zaiou, 2007). Additionally, LL-37 can undergo proteolytic processing to release smaller bioactive fragments with distinct functions (Bowdish et al., 2005).
LL-37's antimicrobial activity extends beyond direct microbial killing. It also exhibits immunomodulatory effects, stimulating the recruitment of immune cells and promoting the clearance of pathogens through phagocytosis (Scott et al., 2002). Furthermore, LL-37 can neutralize endotoxins, reducing inflammation caused by microbial products (Davidson et al., 2004).
LL-37 possesses immunomodulatory properties that influence various immune cells, including neutrophils, macrophages, dendritic cells, and lymphocytes (Nagaoka et al., 2001). It can promote the differentiation and maturation of immune cells, modulate cytokine production, and contribute to wound healing and tissue repair (van Harten et al., 2018).
The multifunctional nature of LL-37 renders it a promising candidate for various therapeutic applications. LL-37-based therapies are being explored in wound healing, infectious diseases, and immune-related disorders (Pena et al., 2014). Furthermore, LL-37 has shown potential as a vaccine adjuvant, enhancing the immune response to antigens (Howell et al., 2018).
LL-37's diverse roles in immunity and host defense warrant further research to unravel its precise mechanisms of action and potential applications in clinical medicine. As we deepen our understanding of LL-37's complexities, its therapeutic potential continues to expand, offering exciting prospects for the future.

What is the molecular weight/Mw of LL-37 Protein?
LL-37 Protein has a total Mw of 4.493kDa.

What is the Purity of LL-37 Protein?
LL-37 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of LL-37 Protein?
The biological functionality of LL-37 Protein will be determined in the future.

What is the amino acid sequence of LL-37 Protein?
H-Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser-OH.

What applications can LL-37 Protein be used in?
LL-37 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for LL-37 Protein?
The endotoxin level is minimal, LL-37 Protein was purified using conventional chromatography techniques.

Who supplies LL-37 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 LL-37?
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:

Tesamorelin

Product # :

HOR-062

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
formulation
purity
More Info
Citations

Description

Tesamorelin is a synthetic single, non-glycosylated polypeptide chain containing 44 amino acids, having a molecular mass of 5135.78 Dalton and a Molecular formula of C221H366N72O67S.

Formulation

The protein was lyophilized with no additives.

Purity

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

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Tesamorelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Tesamorelin 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 Tesamorelin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
trans-3-hexenoyl-Tyr-Ala-Asp-Ala-IlePhe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-LysLeu-Leu-Gln-Asp-Ile-Met-Ser-Arg-Gln-Gln-Gly-Glu-Ser-Asn-Gln-GluArg-Gly-Ala-Arg-Ala-Arg-Leu-NH2.
Background
Tesamorelin is a growth hormone-releasing hormone (GHRH) analogue. Tesamorelin stimulates the pituitary gland to produce endogenous growth hormone, which targets visceral adipose tissue. Tesamorelin has evolved from a HIV treatment into an effective metabolic and regenerative therapy.

What is the molecular weight/Mw of TESAMORELIN Protein?
TESAMORELIN Protein has a total Mw of 5.135kDa.

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

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

What is the amino acid sequence of TESAMORELIN Protein?
trans-3-hexenoyl-Tyr-Ala-Asp-Ala-IlePhe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-LysLeu-Leu-Gln-Asp-Ile-Met-Ser-Arg-Gln-Gln-Gly-Glu-Ser-Asn-Gln-GluArg-Gly-Ala-Arg-Ala-Arg-Leu-NH2.

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

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

Who supplies TESAMORELIN 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 TESAMORELIN?
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:

Stress-Induced Protein SAM22 Recombinant

Stress-induced protein SAM22, Starvation-associated message 22, Gly m 4.

Product # :

PRO-2278

Price :

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.

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.

Description:

Thrombopoietin Mouse Recombinant

Megakaryocyte colony-stimulating factor, Myeloproliferative leukemia virus oncogene ligand, C-mpl ligand, ML, Megakaryocyte growth and development factor, MGDF, TPO, MKCSF, MPLLG, MGC163194, THPO.

Product # :

CYT-346

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Thrombopoietin Mouse Recombinant produced in E.Coli is a single, non-glycosylated soluble polypeptide chain containing 174 amino acids and having a molecular mass of 18704 Dalton. The TPO is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

ED₅₀ range is less than 0.8ng/ml as determined by the dose dependent stimulation of Mo7e cells.

More Info

Introduction
Thrombopoietin is a glycoprotein hormone produced mainly by the liver and the kidneyt hat regulates the production of platelets by the bone marrow. It stimulates the production and differentiation of megakaryocytes, the bone marrow cells that fragment into large numbers of platelets.
Synonyms
Megakaryocyte colony-stimulating factor, Myeloproliferative leukemia virus oncogene ligand, C-mpl ligand, ML, Megakaryocyte growth and development factor, MGDF, TPO, MKCSF, MPLLG, MGC163194, THPO.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Thrombopoietin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TPO Mouse 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 Thrombopoietin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SPVAPACDPR LLNKLLRDSH LLHSRLSQCP DVDPLSIPVL LPAVDFSLGE WKTQTEQSKA QDILGAVSLL LEGVMAARGQ LEPSCLSSLL GQLSGQVRLL LGALQGLLGT QLPLQGRTTA HKDPNALFLS LQQLLRGKVR FLLLVEGPTL CVRRTLPTTA VPSSTSQLLT LNKF.

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 Ovine Recombinant

Mammotropin, Luteotropic hormone, Luteotropin, PRL.

Product # :

CYT-240

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

Prolactin Ovine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids and having a molecular mass of 23 kDa. The Prolactin n is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

Is fully biologically active as evidenced by inducing proliferation of Nb2 cells.

More Info

Introduction
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.
Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Prolactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prl 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 Prolactin in sterile 18MΩ-cm H2O or 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-Thr-Pro-Val-Cys-Pro.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.93 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC DNAman computer analysis program of protein sequences.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Thymus Expressed Chemokine Human Recombinant (CCL25)

C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.

Product # :

CHM-364

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
Citations

Description

TECK Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 14.2kDa. The TECK is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 20mM PB, pH 7.4, 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 human monocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

More Info

Introduction
CCL25 (Teck) is a novel CC chemokine, which is distantly related (about 20% amino acid sequence identity) to other CC chemokines. The mouse CCL25 cDNA has also been cloned and shown to encode a 144 a.a. protein, which exhibits 49% a.a. sequence identity to the human CCL25. Human and mouse CCL25 expression was shown to be greatly restricted to the thymus and small intestine. While dendritic cells are identified as the source of CCL25 production in the thymus, dendritic cells derived from bone marrow do not express CCL25. CCL25 signals through the CCR9 receptor. Teck is possibly involved in T-cell development.
Recombinant human and mouse Teck were shown to be chemotactic for activated macrophages, dendritic cells and thymocytes. The recombinant protein demonstrates chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritic cells but is inactive on peripheral blood lymphocytes and neutrophils.
Synonyms
C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TECK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TECK 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 TECK in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QGVFEDCCLA YHYPIGWAVL RRAWTYRIQE VSGSCNLPAA IFYLPKRHRK VCGNPKSREV QRAMKLLDAR NKVFAKLHHN MQTFQAGPHA VKKLSSGNSK LSSSKFSNPI SSSRKNVSLL ISANSGL.
Background
What is the molecular weight/Mw of CCL25 HUMAN Protein?
CCL25 HUMAN Protein has a total Mw of 14.2kDa.

What is the source or expression system of CCL25 HUMAN Protein?
Escherichia Coli.

What is the Purity of CCL25 HUMAN Protein?
CCL25 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL25 HUMAN Protein?
Determined by its ability to chemoattract human monocytes 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 CCL25 HUMAN Protein?
QGVFEDCCLA YHYPIGWAVL RRAWTYRIQE VSGSCNLPAA IFYLPKRHRK VCGNPKSREV QRAMKLLDAR NKVFAKLHHN MQTFQAGPHA VKKLSSGNSK LSSSKFSNPI SSSRKNVSLL ISANSGL.

What applications can CCL25 HUMAN Protein be used in?
CCL25 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL25 HUMAN Protein?
The endotoxin level is minimal, CCL25 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL25 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CCL25 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Country/region

Search results

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

SDS-PAGE

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Citations

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

Citations

More Info